---
_id: '14835'
abstract:
- lang: ger
text: Aromatische Seitenketten sind wichtige Indikatoren für die Plastizität von
Proteinen und bilden oft entscheidende Kontakte bei Protein‐Protein‐Wechselwirkungen.
Wir untersuchten aromatische Reste in den beiden strukturell homologen cross‐β
Amyloidfibrillen HET‐s und HELLF mit Hilfe eines spezifischen Ansatzes zur Isotopenmarkierung
und Festkörper NMR mit Drehung am magischen Winkel. Das dynamische Verhalten der
aromatischen Reste Phe und Tyr deutet darauf hin, dass der hydrophobe Amyloidkern
starr ist und keine Anzeichen von “atmenden Bewegungen” auf einer Zeitskala von
Hunderten von Millisekunden zeigt. Aromatische Reste, die exponiert an der Fibrillenoberfläche
sitzen, haben zwar eine starre Ringachse, weisen aber Ringflips auf verschiedenen
Zeitskalen von Nanosekunden bis Mikrosekunden auf. Unser Ansatz bietet einen direkten
Einblick in die Bewegungen des hydrophoben Kerns und ermöglicht eine bessere Bewertung
der Konformationsheterogenität, die aus einem NMR‐Strukturensemble einer solchen
Cross‐β‐Amyloidstruktur hervorgeht.
acknowledgement: Wir danken Albert A. Smith (Leipzig) für aufschlussreiche Diskussionen.
Diese Arbeit wurde mit Mitteln des Europäischen Forschungsrats (StG-2012-311318
an P.S.) unterstützt und nutzte die Plattformen des Grenoble Instruct-ERIC Center
(ISBG; UMS 3518 CNRS-CEA-UJF-EMBL) im Rahmen der Grenoble Partnership for Structural
Biology (PSB) sowie die Einrichtungen und das Fachwissen der Biophysical and Structural
Chemistry Platform (BPCS) am IECB, CNRS UAR3033, INSERM US001 und der Universität
Bordeaux.
article_number: e202219314
article_processing_charge: Yes (in subscription journal)
article_type: original
author:
- first_name: Lea Marie
full_name: Becker, Lea Marie
id: 36336939-eb97-11eb-a6c2-c83f1214ca79
last_name: Becker
orcid: 0000-0002-6401-5151
- first_name: Mélanie
full_name: Berbon, Mélanie
last_name: Berbon
- first_name: Alicia
full_name: Vallet, Alicia
last_name: Vallet
- first_name: Axelle
full_name: Grelard, Axelle
last_name: Grelard
- first_name: Estelle
full_name: Morvan, Estelle
last_name: Morvan
- first_name: Benjamin
full_name: Bardiaux, Benjamin
last_name: Bardiaux
- first_name: Roman
full_name: Lichtenecker, Roman
last_name: Lichtenecker
- first_name: Matthias
full_name: Ernst, Matthias
last_name: Ernst
- first_name: Antoine
full_name: Loquet, Antoine
last_name: Loquet
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: Becker LM, Berbon M, Vallet A, et al. Der starre Kern und die flexible Oberfläche
von Amyloidfibrillen – Magic‐Angle‐Spinning NMR Spektroskopie von aromatischen
Resten. Angewandte Chemie. 2023;135(19). doi:10.1002/ange.202219314
apa: Becker, L. M., Berbon, M., Vallet, A., Grelard, A., Morvan, E., Bardiaux, B.,
… Schanda, P. (2023). Der starre Kern und die flexible Oberfläche von Amyloidfibrillen
– Magic‐Angle‐Spinning NMR Spektroskopie von aromatischen Resten. Angewandte
Chemie. Wiley. https://doi.org/10.1002/ange.202219314
chicago: Becker, Lea Marie, Mélanie Berbon, Alicia Vallet, Axelle Grelard, Estelle
Morvan, Benjamin Bardiaux, Roman Lichtenecker, Matthias Ernst, Antoine Loquet,
and Paul Schanda. “Der starre Kern und die flexible Oberfläche von Amyloidfibrillen
– Magic‐Angle‐Spinning NMR Spektroskopie von aromatischen Resten.” Angewandte
Chemie. Wiley, 2023. https://doi.org/10.1002/ange.202219314.
ieee: L. M. Becker et al., “Der starre Kern und die flexible Oberfläche von
Amyloidfibrillen – Magic‐Angle‐Spinning NMR Spektroskopie von aromatischen Resten,”
Angewandte Chemie, vol. 135, no. 19. Wiley, 2023.
ista: Becker LM, Berbon M, Vallet A, Grelard A, Morvan E, Bardiaux B, Lichtenecker
R, Ernst M, Loquet A, Schanda P. 2023. Der starre Kern und die flexible Oberfläche
von Amyloidfibrillen – Magic‐Angle‐Spinning NMR Spektroskopie von aromatischen
Resten. Angewandte Chemie. 135(19), e202219314.
mla: Becker, Lea Marie, et al. “Der starre Kern und die flexible Oberfläche von
Amyloidfibrillen – Magic‐Angle‐Spinning NMR Spektroskopie von aromatischen Resten.”
Angewandte Chemie, vol. 135, no. 19, e202219314, Wiley, 2023, doi:10.1002/ange.202219314.
short: L.M. Becker, M. Berbon, A. Vallet, A. Grelard, E. Morvan, B. Bardiaux, R.
Lichtenecker, M. Ernst, A. Loquet, P. Schanda, Angewandte Chemie 135 (2023).
date_created: 2024-01-18T10:01:01Z
date_published: 2023-05-02T00:00:00Z
date_updated: 2024-01-23T12:23:35Z
day: '02'
ddc:
- '540'
department:
- _id: PaSc
doi: 10.1002/ange.202219314
file:
- access_level: open_access
checksum: 98e68d370159f7be52a3d7c8a8ee1198
content_type: application/pdf
creator: dernst
date_created: 2024-01-23T08:57:01Z
date_updated: 2024-01-23T08:57:01Z
file_id: '14876'
file_name: 2023_AngewChem_Becker.pdf
file_size: 1004676
relation: main_file
success: 1
file_date_updated: 2024-01-23T08:57:01Z
has_accepted_license: '1'
intvolume: ' 135'
issue: '19'
keyword:
- General Medicine
language:
- iso: ger
license: https://creativecommons.org/licenses/by-nc/4.0/
month: '05'
oa: 1
oa_version: Published Version
publication: Angewandte Chemie
publication_identifier:
eissn:
- 1521-3757
issn:
- 0044-8249
publication_status: published
publisher: Wiley
quality_controlled: '1'
status: public
title: Der starre Kern und die flexible Oberfläche von Amyloidfibrillen – Magic‐Angle‐Spinning
NMR Spektroskopie von aromatischen Resten
tmp:
image: /images/cc_by_nc.png
legal_code_url: https://creativecommons.org/licenses/by-nc/4.0/legalcode
name: Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)
short: CC BY-NC (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 135
year: '2023'
...
---
_id: '14847'
abstract:
- lang: eng
text: Understanding the mechanisms of chaperones at the atomic level generally requires
producing chaperone–client complexes in vitro. This task comes with significant
challenges, because one needs to find conditions in which the client protein is
presented to the chaperone in a state that binds and at the same time avoid the
pitfalls of protein aggregation that are often inherent to such states. The strategy
differs significantly for different client proteins and chaperones, but there
are common underlying principles. Here, we discuss these principles and deduce
the strategies that can be successfully applied for different chaperone–client
complexes. We review successful biochemical strategies applied to making the client
protein “binding competent” and illustrate the different strategies with examples
of recent biophysical and biochemical studies.
alternative_title:
- New Developments in NMR
article_processing_charge: No
author:
- first_name: I.
full_name: Sučec, I.
last_name: Sučec
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: 'Sučec I, Schanda P. Preparing Chaperone–Client Protein Complexes for Biophysical
and Structural Studies. In: Hiller S, Liu M, He L, eds. Biophysics of Molecular
Chaperones. Vol 29. Royal Society of Chemistry; 2023:136-161. doi:10.1039/bk9781839165986-00136'
apa: Sučec, I., & Schanda, P. (2023). Preparing Chaperone–Client Protein Complexes
for Biophysical and Structural Studies. In S. Hiller, M. Liu, & L. He (Eds.),
Biophysics of Molecular Chaperones (Vol. 29, pp. 136–161). Royal Society
of Chemistry. https://doi.org/10.1039/bk9781839165986-00136
chicago: Sučec, I., and Paul Schanda. “Preparing Chaperone–Client Protein Complexes
for Biophysical and Structural Studies.” In Biophysics of Molecular Chaperones,
edited by Sebastian Hiller, Maili Liu, and Lichun He, 29:136–61. Royal Society
of Chemistry, 2023. https://doi.org/10.1039/bk9781839165986-00136.
ieee: I. Sučec and P. Schanda, “Preparing Chaperone–Client Protein Complexes for
Biophysical and Structural Studies,” in Biophysics of Molecular Chaperones,
vol. 29, S. Hiller, M. Liu, and L. He, Eds. Royal Society of Chemistry, 2023,
pp. 136–161.
ista: 'Sučec I, Schanda P. 2023.Preparing Chaperone–Client Protein Complexes for
Biophysical and Structural Studies. In: Biophysics of Molecular Chaperones. New
Developments in NMR, vol. 29, 136–161.'
mla: Sučec, I., and Paul Schanda. “Preparing Chaperone–Client Protein Complexes
for Biophysical and Structural Studies.” Biophysics of Molecular Chaperones,
edited by Sebastian Hiller et al., vol. 29, Royal Society of Chemistry, 2023,
pp. 136–61, doi:10.1039/bk9781839165986-00136.
short: I. Sučec, P. Schanda, in:, S. Hiller, M. Liu, L. He (Eds.), Biophysics of
Molecular Chaperones, Royal Society of Chemistry, 2023, pp. 136–161.
date_created: 2024-01-22T08:04:57Z
date_published: 2023-11-01T00:00:00Z
date_updated: 2024-01-23T11:50:10Z
day: '01'
department:
- _id: PaSc
doi: 10.1039/bk9781839165986-00136
editor:
- first_name: Sebastian
full_name: Hiller, Sebastian
last_name: Hiller
- first_name: Maili
full_name: Liu, Maili
last_name: Liu
- first_name: Lichun
full_name: He, Lichun
last_name: He
intvolume: ' 29'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.26434/chemrxiv-2023-rpn28
month: '11'
oa: 1
oa_version: Preprint
page: 136-161
publication: Biophysics of Molecular Chaperones
publication_identifier:
eisbn:
- '9781839165993'
isbn:
- '9781839162824'
publication_status: published
publisher: Royal Society of Chemistry
quality_controlled: '1'
status: public
title: Preparing Chaperone–Client Protein Complexes for Biophysical and Structural
Studies
type: book_chapter
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 29
year: '2023'
...
---
_id: '14861'
abstract:
- lang: eng
text: Cover Page
article_number: ' e202304138'
article_processing_charge: No
author:
- first_name: Lea Marie
full_name: Becker, Lea Marie
id: 36336939-eb97-11eb-a6c2-c83f1214ca79
last_name: Becker
orcid: 0000-0002-6401-5151
- first_name: Mélanie
full_name: Berbon, Mélanie
last_name: Berbon
- first_name: Alicia
full_name: Vallet, Alicia
last_name: Vallet
- first_name: Axelle
full_name: Grelard, Axelle
last_name: Grelard
- first_name: Estelle
full_name: Morvan, Estelle
last_name: Morvan
- first_name: Benjamin
full_name: Bardiaux, Benjamin
last_name: Bardiaux
- first_name: Roman
full_name: Lichtenecker, Roman
last_name: Lichtenecker
- first_name: Matthias
full_name: Ernst, Matthias
last_name: Ernst
- first_name: Antoine
full_name: Loquet, Antoine
last_name: Loquet
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: 'Becker LM, Berbon M, Vallet A, et al. Cover Picture: The Rigid Core and
Flexible Surface of Amyloid Fibrils Probed by Magic‐Angle‐Spinning NMR Spectroscopy
of Aromatic Residues. Vol 62. Wiley; 2023. doi:10.1002/anie.202304138'
apa: 'Becker, L. M., Berbon, M., Vallet, A., Grelard, A., Morvan, E., Bardiaux,
B., … Schanda, P. (2023). Cover Picture: The rigid core and flexible surface
of amyloid fibrils probed by Magic‐Angle‐Spinning NMR spectroscopy of aromatic
residues. Angewandte Chemie International Edition (Vol. 62). Wiley.
https://doi.org/10.1002/anie.202304138'
chicago: 'Becker, Lea Marie, Mélanie Berbon, Alicia Vallet, Axelle Grelard, Estelle
Morvan, Benjamin Bardiaux, Roman Lichtenecker, Matthias Ernst, Antoine Loquet,
and Paul Schanda. Cover Picture: The Rigid Core and Flexible Surface of Amyloid
Fibrils Probed by Magic‐Angle‐Spinning NMR Spectroscopy of Aromatic Residues.
Angewandte Chemie International Edition. Vol. 62. Wiley, 2023. https://doi.org/10.1002/anie.202304138.'
ieee: 'L. M. Becker et al., Cover Picture: The rigid core and flexible
surface of amyloid fibrils probed by Magic‐Angle‐Spinning NMR spectroscopy of
aromatic residues, vol. 62, no. 19. Wiley, 2023.'
ista: 'Becker LM, Berbon M, Vallet A, Grelard A, Morvan E, Bardiaux B, Lichtenecker
R, Ernst M, Loquet A, Schanda P. 2023. Cover Picture: The rigid core and flexible
surface of amyloid fibrils probed by Magic‐Angle‐Spinning NMR spectroscopy of
aromatic residues, Wiley,p.'
mla: 'Becker, Lea Marie, et al. “Cover Picture: The Rigid Core and Flexible Surface
of Amyloid Fibrils Probed by Magic‐Angle‐Spinning NMR Spectroscopy of Aromatic
Residues.” Angewandte Chemie International Edition, vol. 62, no. 19, e202304138,
Wiley, 2023, doi:10.1002/anie.202304138.'
short: 'L.M. Becker, M. Berbon, A. Vallet, A. Grelard, E. Morvan, B. Bardiaux, R.
Lichtenecker, M. Ernst, A. Loquet, P. Schanda, Cover Picture: The Rigid Core and
Flexible Surface of Amyloid Fibrils Probed by Magic‐Angle‐Spinning NMR Spectroscopy
of Aromatic Residues, Wiley, 2023.'
date_created: 2024-01-22T11:54:34Z
date_published: 2023-05-02T00:00:00Z
date_updated: 2024-01-23T08:48:14Z
day: '02'
department:
- _id: PaSc
doi: 10.1002/anie.202304138
intvolume: ' 62'
issue: '19'
keyword:
- General Chemistry
- Catalysis
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1002/anie.202304138
month: '05'
oa: 1
oa_version: Published Version
publication: Angewandte Chemie International Edition
publication_identifier:
eissn:
- 1521-3773
issn:
- 1433-7851
publication_status: published
publisher: Wiley
related_material:
link:
- relation: translation
url: https://doi.org/10.1002/ange.202304138
record:
- id: '12675'
relation: other
status: public
status: public
title: 'Cover Picture: The rigid core and flexible surface of amyloid fibrils probed
by Magic‐Angle‐Spinning NMR spectroscopy of aromatic residues'
type: other_academic_publication
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 62
year: '2023'
...
---
_id: '13095'
abstract:
- lang: eng
text: Disulfide bond formation is fundamentally important for protein structure
and constitutes a key mechanism by which cells regulate the intracellular oxidation
state. Peroxiredoxins (PRDXs) eliminate reactive oxygen species such as hydrogen
peroxide through a catalytic cycle of Cys oxidation and reduction. Additionally,
upon Cys oxidation PRDXs undergo extensive conformational rearrangements that
may underlie their presently structurally poorly defined functions as molecular
chaperones. Rearrangements include high molecular-weight oligomerization, the
dynamics of which are, however, poorly understood, as is the impact of disulfide
bond formation on these properties. Here we show that formation of disulfide bonds
along the catalytic cycle induces extensive μs time scale dynamics, as monitored
by magic-angle spinning NMR of the 216 kDa-large Tsa1 decameric assembly and solution-NMR
of a designed dimeric mutant. We ascribe the conformational dynamics to structural
frustration, resulting from conflicts between the disulfide-constrained reduction
of mobility and the desire to fulfill other favorable contacts.
acknowledgement: "We thank Albert A. Smith (Univ. Leipzig) for discussions and help
with detectors analyses, Undina Guillerm (IST Austria) for gel electrophoresis experiments
(Figure S7), and Jens\r\nLidman (Univ. Gothenburg) for a 3Q relaxation analysis
script. Intramural funding from Institute of Science and Technology Austria is acknowledged.
This work also used the platforms of\r\nthe Grenoble Instruct-ERIC center (ISBG;
UMS 3518 CNRSCEA-UJF-EMBL) within the Grenoble Partnership for Structural Biology
(PSB), as well as the Swedish NMR Centre\r\nof the University of Gothenburg. Both
platforms provided excellent research infrastructures. B.M.B. gratefully acknowledges
funding from the Swedish Research Council (Starting grant 2016-04721), the Swedish
Cancer Foundation (2019-0415), and the Knut och Alice Wallenberg Foundation through
a Wallenberg Academy Fellowship (2016.0163) as well as through the Wallenberg Centre
for Molecular and Translational Medicine, University of Gothenburg, Sweden. "
article_processing_charge: No
article_type: original
author:
- first_name: Laura
full_name: Troussicot, Laura
id: 3d9cac31-413c-11eb-9514-d1ec2a7fb7f3
last_name: Troussicot
- first_name: Alicia
full_name: Vallet, Alicia
last_name: Vallet
- first_name: Mikael
full_name: Molin, Mikael
last_name: Molin
- first_name: Björn M.
full_name: Burmann, Björn M.
last_name: Burmann
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: Troussicot L, Vallet A, Molin M, Burmann BM, Schanda P. Disulfide-bond-induced
structural frustration and dynamic disorder in a peroxiredoxin from MAS NMR. Journal
of the American Chemical Society. 2023;145(19):10700–10711. doi:10.1021/jacs.3c01200
apa: Troussicot, L., Vallet, A., Molin, M., Burmann, B. M., & Schanda, P. (2023).
Disulfide-bond-induced structural frustration and dynamic disorder in a peroxiredoxin
from MAS NMR. Journal of the American Chemical Society. American Chemical
Society. https://doi.org/10.1021/jacs.3c01200
chicago: Troussicot, Laura, Alicia Vallet, Mikael Molin, Björn M. Burmann, and Paul
Schanda. “Disulfide-Bond-Induced Structural Frustration and Dynamic Disorder in
a Peroxiredoxin from MAS NMR.” Journal of the American Chemical Society.
American Chemical Society, 2023. https://doi.org/10.1021/jacs.3c01200.
ieee: L. Troussicot, A. Vallet, M. Molin, B. M. Burmann, and P. Schanda, “Disulfide-bond-induced
structural frustration and dynamic disorder in a peroxiredoxin from MAS NMR,”
Journal of the American Chemical Society, vol. 145, no. 19. American Chemical
Society, pp. 10700–10711, 2023.
ista: Troussicot L, Vallet A, Molin M, Burmann BM, Schanda P. 2023. Disulfide-bond-induced
structural frustration and dynamic disorder in a peroxiredoxin from MAS NMR. Journal
of the American Chemical Society. 145(19), 10700–10711.
mla: Troussicot, Laura, et al. “Disulfide-Bond-Induced Structural Frustration and
Dynamic Disorder in a Peroxiredoxin from MAS NMR.” Journal of the American
Chemical Society, vol. 145, no. 19, American Chemical Society, 2023, pp. 10700–10711,
doi:10.1021/jacs.3c01200.
short: L. Troussicot, A. Vallet, M. Molin, B.M. Burmann, P. Schanda, Journal of
the American Chemical Society 145 (2023) 10700–10711.
date_created: 2023-05-28T22:01:04Z
date_published: 2023-05-04T00:00:00Z
date_updated: 2023-08-01T14:48:09Z
day: '04'
ddc:
- '540'
department:
- _id: PaSc
doi: 10.1021/jacs.3c01200
external_id:
isi:
- '000985907400001'
pmid:
- '37140345'
file:
- access_level: open_access
checksum: 0758a930ef21c62fc91b14e657479f83
content_type: application/pdf
creator: dernst
date_created: 2023-05-30T07:05:28Z
date_updated: 2023-05-30T07:05:28Z
file_id: '13098'
file_name: 2023_JACS_Troussicot.pdf
file_size: 6719299
relation: main_file
success: 1
file_date_updated: 2023-05-30T07:05:28Z
has_accepted_license: '1'
intvolume: ' 145'
isi: 1
issue: '19'
language:
- iso: eng
license: https://creativecommons.org/licenses/by/4.0/
month: '05'
oa: 1
oa_version: Published Version
page: 10700–10711
pmid: 1
publication: Journal of the American Chemical Society
publication_identifier:
eissn:
- 1520-5126
issn:
- 0002-7863
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
related_material:
record:
- id: '12820'
relation: research_data
status: public
scopus_import: '1'
status: public
title: Disulfide-bond-induced structural frustration and dynamic disorder in a peroxiredoxin
from MAS NMR
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 145
year: '2023'
...
---
_id: '13096'
abstract:
- lang: eng
text: Eukaryotic cells can undergo different forms of programmed cell death, many
of which culminate in plasma membrane rupture as the defining terminal event1,2,3,4,5,6,7.
Plasma membrane rupture was long thought to be driven by osmotic pressure, but
it has recently been shown to be in many cases an active process, mediated by
the protein ninjurin-18 (NINJ1). Here we resolve the structure of NINJ1 and the
mechanism by which it ruptures membranes. Super-resolution microscopy reveals
that NINJ1 clusters into structurally diverse assemblies in the membranes of dying
cells, in particular large, filamentous assemblies with branched morphology. A
cryo-electron microscopy structure of NINJ1 filaments shows a tightly packed fence-like
array of transmembrane α-helices. Filament directionality and stability is defined
by two amphipathic α-helices that interlink adjacent filament subunits. The NINJ1
filament features a hydrophilic side and a hydrophobic side, and molecular dynamics
simulations show that it can stably cap membrane edges. The function of the resulting
supramolecular arrangement was validated by site-directed mutagenesis. Our data
thus suggest that, during lytic cell death, the extracellular α-helices of NINJ1
insert into the plasma membrane to polymerize NINJ1 monomers into amphipathic
filaments that rupture the plasma membrane. The membrane protein NINJ1 is therefore
an interactive component of the eukaryotic cell membrane that functions as an
in-built breaking point in response to activation of cell death.
acknowledged_ssus:
- _id: NMR
- _id: LifeSc
acknowledgement: "This work was supported by the Deutsche Forschungsgemeinschaft under
Germany’s Excellence Strategy EXC 2075–390740016 and the Stuttgart Center for Simulation
Science (SC SimTech) to K.P., by ERC-CoG 770988 (InflamCellDeath) and SNF Project
funding (310030B_198005, 310030B_192523) to P.B., by the Swiss Nanoscience Institute
and the Swiss National Science Foundation via the NCCR AntiResist (180541) to S.H.
and the NCCR Molecular Systems Engineering (51NF40-205608) to D.J.M., by the Helmholtz
Young Investigator Program of the Helmholtz Association to C.S., by the SNF Professorship
funding (PP00P3_198903) to C.P., EMBO postdoctoral fellowship ALTF 27-2022 to E.H.
and by the Scientific Service Units of IST Austria through resources provided by
the NMR and Life Science Facilities to P.S. Molecular dynamics simulations were
performed on the HoreKa supercomputer funded by the Ministry of Science, Research
and the Arts Baden-Württemberg and by the Federal Ministry of Education and Research.
The authors thank the BioEM Lab of the Biozentrum, University of Basel for support;
V. Mack, K. Shkarina and J. Fricke for technical support; D. Ricklin and S. Vogt
for peptide synthesis; P. Pelczar for support with animals; S.-J. Marrink and P.
Telles de Souza for supply with Martini3 parameters and scripts; and P. Radler und
M. Loose for help with QCM. Fig. 4g and Extended Data Fig. 1a were in part created
with BioRender.com.\r\nOpen access funding provided by University of Basel."
article_processing_charge: Yes (via OA deal)
article_type: original
author:
- first_name: Morris
full_name: Degen, Morris
last_name: Degen
- first_name: José Carlos
full_name: Santos, José Carlos
last_name: Santos
- first_name: Kristyna
full_name: Pluhackova, Kristyna
last_name: Pluhackova
- first_name: Gonzalo
full_name: Cebrero, Gonzalo
last_name: Cebrero
- first_name: Saray
full_name: Ramos, Saray
last_name: Ramos
- first_name: Gytis
full_name: Jankevicius, Gytis
last_name: Jankevicius
- first_name: Ella
full_name: Hartenian, Ella
last_name: Hartenian
- first_name: Undina
full_name: Guillerm, Undina
id: bb74f472-ae54-11eb-9835-bc9c22fb1183
last_name: Guillerm
- first_name: Stefania A.
full_name: Mari, Stefania A.
last_name: Mari
- first_name: Bastian
full_name: Kohl, Bastian
last_name: Kohl
- first_name: Daniel J.
full_name: Müller, Daniel J.
last_name: Müller
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Timm
full_name: Maier, Timm
last_name: Maier
- first_name: Camilo
full_name: Perez, Camilo
last_name: Perez
- first_name: Christian
full_name: Sieben, Christian
last_name: Sieben
- first_name: Petr
full_name: Broz, Petr
last_name: Broz
- first_name: Sebastian
full_name: Hiller, Sebastian
last_name: Hiller
citation:
ama: Degen M, Santos JC, Pluhackova K, et al. Structural basis of NINJ1-mediated
plasma membrane rupture in cell death. Nature. 2023;618:1065-1071. doi:10.1038/s41586-023-05991-z
apa: Degen, M., Santos, J. C., Pluhackova, K., Cebrero, G., Ramos, S., Jankevicius,
G., … Hiller, S. (2023). Structural basis of NINJ1-mediated plasma membrane rupture
in cell death. Nature. Springer Nature. https://doi.org/10.1038/s41586-023-05991-z
chicago: Degen, Morris, José Carlos Santos, Kristyna Pluhackova, Gonzalo Cebrero,
Saray Ramos, Gytis Jankevicius, Ella Hartenian, et al. “Structural Basis of NINJ1-Mediated
Plasma Membrane Rupture in Cell Death.” Nature. Springer Nature, 2023.
https://doi.org/10.1038/s41586-023-05991-z.
ieee: M. Degen et al., “Structural basis of NINJ1-mediated plasma membrane
rupture in cell death,” Nature, vol. 618. Springer Nature, pp. 1065–1071,
2023.
ista: Degen M, Santos JC, Pluhackova K, Cebrero G, Ramos S, Jankevicius G, Hartenian
E, Guillerm U, Mari SA, Kohl B, Müller DJ, Schanda P, Maier T, Perez C, Sieben
C, Broz P, Hiller S. 2023. Structural basis of NINJ1-mediated plasma membrane
rupture in cell death. Nature. 618, 1065–1071.
mla: Degen, Morris, et al. “Structural Basis of NINJ1-Mediated Plasma Membrane Rupture
in Cell Death.” Nature, vol. 618, Springer Nature, 2023, pp. 1065–71, doi:10.1038/s41586-023-05991-z.
short: M. Degen, J.C. Santos, K. Pluhackova, G. Cebrero, S. Ramos, G. Jankevicius,
E. Hartenian, U. Guillerm, S.A. Mari, B. Kohl, D.J. Müller, P. Schanda, T. Maier,
C. Perez, C. Sieben, P. Broz, S. Hiller, Nature 618 (2023) 1065–1071.
date_created: 2023-05-28T22:01:04Z
date_published: 2023-06-29T00:00:00Z
date_updated: 2023-11-14T11:49:21Z
day: '29'
ddc:
- '570'
department:
- _id: PaSc
doi: 10.1038/s41586-023-05991-z
external_id:
isi:
- '000991386800011'
file:
- access_level: open_access
checksum: 0fab69252453bff1de7f0e2eceb76d34
content_type: application/pdf
creator: dernst
date_created: 2023-11-14T11:48:18Z
date_updated: 2023-11-14T11:48:18Z
file_id: '14533'
file_name: 2023_Nature_Degen.pdf
file_size: 12292188
relation: main_file
success: 1
file_date_updated: 2023-11-14T11:48:18Z
has_accepted_license: '1'
intvolume: ' 618'
isi: 1
language:
- iso: eng
month: '06'
oa: 1
oa_version: Published Version
page: 1065-1071
publication: Nature
publication_identifier:
eissn:
- 1476-4687
issn:
- 0028-0836
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: Structural basis of NINJ1-mediated plasma membrane rupture in cell death
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 618
year: '2023'
...
---
_id: '14036'
abstract:
- lang: eng
text: Magic-angle spinning (MAS) nuclear magnetic resonance (NMR) is establishing
itself as a powerful method for the characterization of protein dynamics at the
atomic scale. We discuss here how R1ρ MAS relaxation dispersion NMR can explore
microsecond-to-millisecond motions. Progress in instrumentation, isotope labeling,
and pulse sequence design has paved the way for quantitative analyses of even
rare structural fluctuations. In addition to isotropic chemical-shift fluctuations
exploited in solution-state NMR relaxation dispersion experiments, MAS NMR has
a wider arsenal of observables, allowing to see motions even if the exchanging
states do not differ in their chemical shifts. We demonstrate the potential of
the technique for probing motions in challenging large enzymes, membrane proteins,
and protein assemblies.
acknowledgement: We thank Petra Rovó for critical reading of this manuscript. We acknowledge
the Austrian Science Foundation FWF (project AlloSpace, number I5812–B) and funding
by the Institute of Science and Technology Austria.
article_number: '102660'
article_processing_charge: Yes (via OA deal)
article_type: original
author:
- first_name: Federico
full_name: Napoli, Federico
id: d42e08e7-f4fc-11eb-af0a-d71e26138f1b
last_name: Napoli
orcid: 0000-0002-9043-136X
- first_name: Lea Marie
full_name: Becker, Lea Marie
id: 36336939-eb97-11eb-a6c2-c83f1214ca79
last_name: Becker
orcid: 0000-0002-6401-5151
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: Napoli F, Becker LM, Schanda P. Protein dynamics detected by magic-angle spinning
relaxation dispersion NMR. Current Opinion in Structural Biology. 2023;82(10).
doi:10.1016/j.sbi.2023.102660
apa: Napoli, F., Becker, L. M., & Schanda, P. (2023). Protein dynamics detected
by magic-angle spinning relaxation dispersion NMR. Current Opinion in Structural
Biology. Elsevier. https://doi.org/10.1016/j.sbi.2023.102660
chicago: Napoli, Federico, Lea Marie Becker, and Paul Schanda. “Protein Dynamics
Detected by Magic-Angle Spinning Relaxation Dispersion NMR.” Current Opinion
in Structural Biology. Elsevier, 2023. https://doi.org/10.1016/j.sbi.2023.102660.
ieee: F. Napoli, L. M. Becker, and P. Schanda, “Protein dynamics detected by magic-angle
spinning relaxation dispersion NMR,” Current Opinion in Structural Biology,
vol. 82, no. 10. Elsevier, 2023.
ista: Napoli F, Becker LM, Schanda P. 2023. Protein dynamics detected by magic-angle
spinning relaxation dispersion NMR. Current Opinion in Structural Biology. 82(10),
102660.
mla: Napoli, Federico, et al. “Protein Dynamics Detected by Magic-Angle Spinning
Relaxation Dispersion NMR.” Current Opinion in Structural Biology, vol.
82, no. 10, 102660, Elsevier, 2023, doi:10.1016/j.sbi.2023.102660.
short: F. Napoli, L.M. Becker, P. Schanda, Current Opinion in Structural Biology
82 (2023).
date_created: 2023-08-13T22:01:11Z
date_published: 2023-10-01T00:00:00Z
date_updated: 2024-01-30T12:37:36Z
day: '01'
ddc:
- '570'
department:
- _id: PaSc
doi: 10.1016/j.sbi.2023.102660
external_id:
isi:
- '001053616200001'
pmid:
- '37536064'
file:
- access_level: open_access
checksum: c850f7ac8a4234319755b672c1df69ae
content_type: application/pdf
creator: dernst
date_created: 2024-01-30T12:36:39Z
date_updated: 2024-01-30T12:36:39Z
file_id: '14907'
file_name: 2023_CurrentOpinionStrucBio_Napoli.pdf
file_size: 1231998
relation: main_file
success: 1
file_date_updated: 2024-01-30T12:36:39Z
intvolume: ' 82'
isi: 1
issue: '10'
language:
- iso: eng
month: '10'
oa: 1
oa_version: Published Version
pmid: 1
project:
- _id: eb9c82eb-77a9-11ec-83b8-aadd536561cf
grant_number: I05812
name: AlloSpace. The emergence and mechanisms of allostery
publication: Current Opinion in Structural Biology
publication_identifier:
eissn:
- 1879-033X
issn:
- 0959-440X
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Protein dynamics detected by magic-angle spinning relaxation dispersion NMR
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 82
year: '2023'
...
---
_id: '12114'
abstract:
- lang: eng
text: 'Probing the dynamics of aromatic side chains provides important insights
into the behavior of a protein because flips of aromatic rings in a protein’s
hydrophobic core report on breathing motion involving a large part of the protein.
Inherently invisible to crystallography, aromatic motions have been primarily
studied by solution NMR. The question how packing of proteins in crystals affects
ring flips has, thus, remained largely unexplored. Here we apply magic-angle spinning
NMR, advanced phenylalanine 1H-13C/2H isotope labeling and MD simulation to a
protein in three different crystal packing environments to shed light onto possible
impact of packing on ring flips. The flips of the two Phe residues in ubiquitin,
both surface exposed, appear remarkably conserved in the different crystal forms,
even though the intermolecular packing is quite different: Phe4 flips on a ca.
10–20 ns time scale, and Phe45 are broadened in all crystals, presumably due to
µs motion. Our findings suggest that intramolecular influences are more important
for ring flips than intermolecular (packing) effects.'
acknowledgement: The NMR platform in Grenoble is part of the Grenoble Instruct-ERIC
center (ISBG; UAR 3518 CNRS-CEA-UGA-EMBL) within the Grenoble Partnership for Structural
Biology (PSB), supported by FRISBI (ANR-10-INBS-0005-02) and GRAL, financed within
the University Grenoble Alpes graduate school (Ecoles Universitaires de Recherche)
CBH-EUR-GS (ANR-17-EURE-0003). This work was supported by the European Research
Council (StG-2012-311318-ProtDyn2Function to P.S.) and used the platforms of the
Grenoble Instruct Center (ISBG; UMS 3518 CNRS-CEA-UJF-EMBL) with support from FRISBI
(ANR-10-INSB-05–02) and GRAL (ANR-10-LABX-49–01) within the Grenoble Partnership
for Structural Biology (PSB). We would like to thank Sergei Izmailov for developing
and maintaining the pyxmolpp2 library. N.R.S. acknowledges support from St. Petersburg
State University in a form of the grant 92425251 and the access to the MRR, MCT
and CAMR resource centers. P.S. thanks Malcolm Levitt for pointing out the fact
that “tensor asymmetry” is better called “tensor biaxiality”.
article_number: '100079'
article_processing_charge: No
article_type: original
author:
- first_name: Diego F.
full_name: Gauto, Diego F.
last_name: Gauto
- first_name: Olga O.
full_name: Lebedenko, Olga O.
last_name: Lebedenko
- first_name: Lea Marie
full_name: Becker, Lea Marie
id: 36336939-eb97-11eb-a6c2-c83f1214ca79
last_name: Becker
orcid: 0000-0002-6401-5151
- first_name: Isabel
full_name: Ayala, Isabel
last_name: Ayala
- first_name: Roman
full_name: Lichtenecker, Roman
last_name: Lichtenecker
- first_name: Nikolai R.
full_name: Skrynnikov, Nikolai R.
last_name: Skrynnikov
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: 'Gauto DF, Lebedenko OO, Becker LM, et al. Aromatic ring flips in differently
packed ubiquitin protein crystals from MAS NMR and MD. Journal of Structural
Biology: X. 2023;7. doi:10.1016/j.yjsbx.2022.100079'
apa: 'Gauto, D. F., Lebedenko, O. O., Becker, L. M., Ayala, I., Lichtenecker, R.,
Skrynnikov, N. R., & Schanda, P. (2023). Aromatic ring flips in differently
packed ubiquitin protein crystals from MAS NMR and MD. Journal of Structural
Biology: X. Elsevier. https://doi.org/10.1016/j.yjsbx.2022.100079'
chicago: 'Gauto, Diego F., Olga O. Lebedenko, Lea Marie Becker, Isabel Ayala, Roman
Lichtenecker, Nikolai R. Skrynnikov, and Paul Schanda. “Aromatic Ring Flips in
Differently Packed Ubiquitin Protein Crystals from MAS NMR and MD.” Journal
of Structural Biology: X. Elsevier, 2023. https://doi.org/10.1016/j.yjsbx.2022.100079.'
ieee: 'D. F. Gauto et al., “Aromatic ring flips in differently packed ubiquitin
protein crystals from MAS NMR and MD,” Journal of Structural Biology: X,
vol. 7. Elsevier, 2023.'
ista: 'Gauto DF, Lebedenko OO, Becker LM, Ayala I, Lichtenecker R, Skrynnikov NR,
Schanda P. 2023. Aromatic ring flips in differently packed ubiquitin protein crystals
from MAS NMR and MD. Journal of Structural Biology: X. 7, 100079.'
mla: 'Gauto, Diego F., et al. “Aromatic Ring Flips in Differently Packed Ubiquitin
Protein Crystals from MAS NMR and MD.” Journal of Structural Biology: X,
vol. 7, 100079, Elsevier, 2023, doi:10.1016/j.yjsbx.2022.100079.'
short: 'D.F. Gauto, O.O. Lebedenko, L.M. Becker, I. Ayala, R. Lichtenecker, N.R.
Skrynnikov, P. Schanda, Journal of Structural Biology: X 7 (2023).'
date_created: 2023-01-12T11:55:38Z
date_published: 2023-01-01T00:00:00Z
date_updated: 2023-08-16T09:37:25Z
day: '01'
ddc:
- '570'
department:
- _id: PaSc
doi: 10.1016/j.yjsbx.2022.100079
external_id:
pmid:
- '36578472'
file:
- access_level: open_access
checksum: b4b1c10a31018aafe053b7d55a470e54
content_type: application/pdf
creator: dernst
date_created: 2023-08-16T09:36:28Z
date_updated: 2023-08-16T09:36:28Z
file_id: '14064'
file_name: 2023_JourStrucBiologyX_Gauto.pdf
file_size: 5132322
relation: main_file
success: 1
file_date_updated: 2023-08-16T09:36:28Z
has_accepted_license: '1'
intvolume: ' 7'
keyword:
- Structural Biology
language:
- iso: eng
license: https://creativecommons.org/licenses/by-nc-nd/4.0/
month: '01'
oa: 1
oa_version: Published Version
pmid: 1
publication: 'Journal of Structural Biology: X'
publication_identifier:
issn:
- 2590-1524
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Aromatic ring flips in differently packed ubiquitin protein crystals from MAS
NMR and MD
tmp:
image: /images/cc_by_nc_nd.png
legal_code_url: https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode
name: Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International
(CC BY-NC-ND 4.0)
short: CC BY-NC-ND (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 7
year: '2023'
...
---
_id: '12497'
abstract:
- lang: eng
text: Aromatic side chains are important reporters of the plasticity of proteins,
and often form important contacts in protein–protein interactions. We studied
aromatic residues in the two structurally homologous cross-β amyloid fibrils HET-s,
and HELLF by employing a specific isotope-labeling approach and magic-angle-spinning
NMR. The dynamic behavior of the aromatic residues Phe and Tyr indicates that
the hydrophobic amyloid core is rigid, without any sign of "breathing motions"
over hundreds of milliseconds at least. Aromatic residues exposed at the fibril
surface have a rigid ring axis but undergo ring flips on a variety of time scales
from nanoseconds to microseconds. Our approach provides direct insight into hydrophobic-core
motions, enabling a better evaluation of the conformational heterogeneity generated
from an NMR structural ensemble of such amyloid cross-β architecture.
article_processing_charge: No
author:
- first_name: Lea Marie
full_name: Becker, Lea Marie
id: 36336939-eb97-11eb-a6c2-c83f1214ca79
last_name: Becker
orcid: 0000-0002-6401-5151
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: 'Becker LM, Schanda P. Research data to: The rigid core and flexible surface
of amyloid fibrils probed by magic-angle-spinning NMR spectroscopy of aromatic
residues. 2023. doi:10.15479/AT:ISTA:12497'
apa: 'Becker, L. M., & Schanda, P. (2023). Research data to: The rigid core
and flexible surface of amyloid fibrils probed by magic-angle-spinning NMR spectroscopy
of aromatic residues. Institute of Science and Technology Austria. https://doi.org/10.15479/AT:ISTA:12497'
chicago: 'Becker, Lea Marie, and Paul Schanda. “Research Data to: The Rigid Core
and Flexible Surface of Amyloid Fibrils Probed by Magic-Angle-Spinning NMR Spectroscopy
of Aromatic Residues.” Institute of Science and Technology Austria, 2023. https://doi.org/10.15479/AT:ISTA:12497.'
ieee: 'L. M. Becker and P. Schanda, “Research data to: The rigid core and flexible
surface of amyloid fibrils probed by magic-angle-spinning NMR spectroscopy of
aromatic residues.” Institute of Science and Technology Austria, 2023.'
ista: 'Becker LM, Schanda P. 2023. Research data to: The rigid core and flexible
surface of amyloid fibrils probed by magic-angle-spinning NMR spectroscopy of
aromatic residues, Institute of Science and Technology Austria, 10.15479/AT:ISTA:12497.'
mla: 'Becker, Lea Marie, and Paul Schanda. Research Data to: The Rigid Core and
Flexible Surface of Amyloid Fibrils Probed by Magic-Angle-Spinning NMR Spectroscopy
of Aromatic Residues. Institute of Science and Technology Austria, 2023, doi:10.15479/AT:ISTA:12497.'
short: L.M. Becker, P. Schanda, (2023).
contributor:
- contributor_type: researcher
first_name: Mélanie
last_name: Berbon
- contributor_type: researcher
first_name: Alicia
last_name: Vallet
- contributor_type: researcher
first_name: Axelle
last_name: Grelard
- contributor_type: researcher
first_name: Estelle
last_name: Morvan
- contributor_type: researcher
first_name: Benjamin
last_name: Bardiaux
- contributor_type: researcher
first_name: Roman
last_name: Lichtenecker
- contributor_type: researcher
first_name: Matthias
last_name: Ernst
- contributor_type: researcher
first_name: Antoine
last_name: Loquet
- contributor_type: contact_person
first_name: Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- contributor_type: researcher
first_name: Lea Marie
id: 36336939-eb97-11eb-a6c2-c83f1214ca79
last_name: Becker
orcid: 0000-0002-6401-5151
date_created: 2023-02-03T08:08:02Z
date_published: 2023-03-23T00:00:00Z
date_updated: 2024-02-21T12:14:06Z
day: '23'
ddc:
- '572'
department:
- _id: GradSch
- _id: PaSc
doi: 10.15479/AT:ISTA:12497
file:
- access_level: open_access
checksum: fd9a28620a81a82991fb70f4fd6591d9
content_type: application/zip
creator: lbecker
date_created: 2023-03-23T10:03:16Z
date_updated: 2023-03-24T09:34:20Z
file_id: '12743'
file_name: Research_Data.zip
file_size: 87018103
relation: main_file
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checksum: 30ebdfb600af118fcf8518b6efe0b7e9
content_type: text/plain
creator: dernst
date_created: 2023-03-24T07:13:55Z
date_updated: 2023-03-24T09:42:03Z
file_id: '12755'
file_name: README.txt
file_size: 747
relation: main_file
file_date_updated: 2023-03-24T09:42:03Z
has_accepted_license: '1'
keyword:
- aromatic side chains
- isotopic labeling
- protein dynamics
- ring flips
- spin relaxation
month: '03'
oa: 1
oa_version: Published Version
publisher: Institute of Science and Technology Austria
related_material:
record:
- id: '12675'
relation: used_in_publication
status: public
status: public
title: 'Research data to: The rigid core and flexible surface of amyloid fibrils probed
by magic-angle-spinning NMR spectroscopy of aromatic residues'
tmp:
image: /images/cc_by_nc.png
legal_code_url: https://creativecommons.org/licenses/by-nc/4.0/legalcode
name: Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)
short: CC BY-NC (4.0)
type: research_data
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
year: '2023'
...
---
_id: '12675'
abstract:
- lang: eng
text: Aromatic side chains are important reporters of the plasticity of proteins,
and often form important contacts in protein--protein interactions. By studying
a pair of structurally homologous cross-β amyloid fibrils, HET-s and HELLF, with
a specific isotope-labeling approach and magic-angle-spinning (MAS) NMR, we have
characterized the dynamic behavior of Phe and Tyr aromatic rings to show that
the hydrophobic amyloid core is rigid, without any sign of "breathing motions"
over hundreds of milliseconds at least. Aromatic residues exposed at the fibril
surface have a rigid ring axis but undergo ring flips, on a variety of time scales
from ns to µs. Our approach provides direct insight into hydrophobic-core motions,
enabling a better evaluation of the conformational heterogeneity generated from
a NMR structural ensemble of such amyloid cross-β architecture.
acknowledgement: We thank AlbertA. Smith (Leipzig)for insightful discussions. This
work was supported by funding from the European Research Council (StG-2012-311318
to P.S.) and used the platforms of the Grenoble Instruct-ERIC center (ISBG;UMS 3518
CNRS-CEA-UJF-EMBL) within the Grenoble Partnership for Structural Biology(PSB) and
facilities and expertiseof the Biophysical and Structural Chemistry platform (BPCS)
at IECB,CNRSUAR3033,INSERMUS001 and Bordeaux University.
article_number: e202219314
article_processing_charge: Yes (via OA deal)
article_type: original
author:
- first_name: Lea Marie
full_name: Becker, Lea Marie
id: 36336939-eb97-11eb-a6c2-c83f1214ca79
last_name: Becker
orcid: 0000-0002-6401-5151
- first_name: Mélanie
full_name: Berbon, Mélanie
last_name: Berbon
- first_name: Alicia
full_name: Vallet, Alicia
last_name: Vallet
- first_name: Axelle
full_name: Grelard, Axelle
last_name: Grelard
- first_name: Estelle
full_name: Morvan, Estelle
last_name: Morvan
- first_name: Benjamin
full_name: Bardiaux, Benjamin
last_name: Bardiaux
- first_name: Roman
full_name: Lichtenecker, Roman
last_name: Lichtenecker
- first_name: Matthias
full_name: Ernst, Matthias
last_name: Ernst
- first_name: Antoine
full_name: Loquet, Antoine
last_name: Loquet
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: Becker LM, Berbon M, Vallet A, et al. The rigid core and flexible surface of
amyloid fibrils probed by Magic‐Angle Spinning NMR of aromatic residues. Angewandte
Chemie International Edition. 2023;62(19). doi:10.1002/anie.202219314
apa: Becker, L. M., Berbon, M., Vallet, A., Grelard, A., Morvan, E., Bardiaux, B.,
… Schanda, P. (2023). The rigid core and flexible surface of amyloid fibrils probed
by Magic‐Angle Spinning NMR of aromatic residues. Angewandte Chemie International
Edition. Wiley. https://doi.org/10.1002/anie.202219314
chicago: Becker, Lea Marie, Mélanie Berbon, Alicia Vallet, Axelle Grelard, Estelle
Morvan, Benjamin Bardiaux, Roman Lichtenecker, Matthias Ernst, Antoine Loquet,
and Paul Schanda. “The Rigid Core and Flexible Surface of Amyloid Fibrils Probed
by Magic‐Angle Spinning NMR of Aromatic Residues.” Angewandte Chemie International
Edition. Wiley, 2023. https://doi.org/10.1002/anie.202219314.
ieee: L. M. Becker et al., “The rigid core and flexible surface of amyloid
fibrils probed by Magic‐Angle Spinning NMR of aromatic residues,” Angewandte
Chemie International Edition, vol. 62, no. 19. Wiley, 2023.
ista: Becker LM, Berbon M, Vallet A, Grelard A, Morvan E, Bardiaux B, Lichtenecker
R, Ernst M, Loquet A, Schanda P. 2023. The rigid core and flexible surface of
amyloid fibrils probed by Magic‐Angle Spinning NMR of aromatic residues. Angewandte
Chemie International Edition. 62(19), e202219314.
mla: Becker, Lea Marie, et al. “The Rigid Core and Flexible Surface of Amyloid Fibrils
Probed by Magic‐Angle Spinning NMR of Aromatic Residues.” Angewandte Chemie
International Edition, vol. 62, no. 19, e202219314, Wiley, 2023, doi:10.1002/anie.202219314.
short: L.M. Becker, M. Berbon, A. Vallet, A. Grelard, E. Morvan, B. Bardiaux, R.
Lichtenecker, M. Ernst, A. Loquet, P. Schanda, Angewandte Chemie International
Edition 62 (2023).
date_created: 2023-02-24T10:45:01Z
date_published: 2023-05-01T00:00:00Z
date_updated: 2024-02-21T12:14:06Z
day: '01'
ddc:
- '540'
department:
- _id: GradSch
- _id: PaSc
doi: 10.1002/anie.202219314
external_id:
isi:
- '000956919900001'
pmid:
- '36738230'
file:
- access_level: open_access
checksum: 7dd083ed8850faa55c34e411ed390de9
content_type: application/pdf
creator: dernst
date_created: 2023-08-16T12:33:31Z
date_updated: 2023-08-16T12:33:31Z
file_id: '14072'
file_name: 2023_AngewChemInt_Becker.pdf
file_size: 1422445
relation: main_file
success: 1
file_date_updated: 2023-08-16T12:33:31Z
has_accepted_license: '1'
intvolume: ' 62'
isi: 1
issue: '19'
keyword:
- General Chemistry
- Catalysis
language:
- iso: eng
month: '05'
oa: 1
oa_version: Published Version
pmid: 1
publication: Angewandte Chemie International Edition
publication_identifier:
eissn:
- 1521-3773
issn:
- 1433-7851
publication_status: published
publisher: Wiley
quality_controlled: '1'
related_material:
link:
- description: News on ISTA website
relation: press_release
url: https://ista.ac.at/en/news/dancing-styles-of-atoms/
record:
- id: '14861'
relation: other
status: public
- id: '12497'
relation: research_data
status: public
status: public
title: The rigid core and flexible surface of amyloid fibrils probed by Magic‐Angle
Spinning NMR of aromatic residues
tmp:
image: /images/cc_by_nc.png
legal_code_url: https://creativecommons.org/licenses/by-nc/4.0/legalcode
name: Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)
short: CC BY-NC (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 62
year: '2023'
...
---
_id: '12820'
abstract:
- lang: eng
text: "Disulfide bond formation is fundamentally important for protein structure,
and constitutes a key mechanism by which cells regulate the intracellular oxidation
state. Peroxiredoxins (PRDXs) eliminate reactive oxygen species such as hydrogen
peroxide through a catalytic cycle of Cys oxidation and reduction. Additionally,
upon Cys oxidation PRDXs undergo extensive conformational rearrangements that
may underlie their presently structurally poorly defined functions as molecular
chaperones. Rearrangements include high molecular-weight oligomerization, the
dynamics of which are, however, poorly understood, as is the impact of disulfide
bond formation on these properties. Here we show that formation of disulfide bonds
along the catalytic cycle induces extensive microsecond time scale dynamics, as
monitored by magic-angle spinning NMR of the 216 kDa-large Tsa1 decameric assembly
and solution-NMR of a designed dimeric mutant. We ascribe the conformational dynamics
to structural frustration, resulting from conflicts between the disulfide-constrained
reduction of mobility and the desire to fulfil other favorable contacts. \r\n\r\nThis
data repository contains NMR data presented in the associated manuscript"
article_processing_charge: No
author:
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: Schanda P. Research data of the publication “Disulfide-bond-induced structural
frustration and dynamic disorder in a peroxiredoxin from MAS NMR.” 2023. doi:10.15479/AT:ISTA:12820
apa: Schanda, P. (2023). Research data of the publication “Disulfide-bond-induced
structural frustration and dynamic disorder in a peroxiredoxin from MAS NMR.”
Institute of Science and Technology Austria. https://doi.org/10.15479/AT:ISTA:12820
chicago: Schanda, Paul. “Research Data of the Publication ‘Disulfide-Bond-Induced
Structural Frustration and Dynamic Disorder in a Peroxiredoxin from MAS NMR.’”
Institute of Science and Technology Austria, 2023. https://doi.org/10.15479/AT:ISTA:12820.
ieee: P. Schanda, “Research data of the publication ‘Disulfide-bond-induced structural
frustration and dynamic disorder in a peroxiredoxin from MAS NMR.’” Institute
of Science and Technology Austria, 2023.
ista: Schanda P. 2023. Research data of the publication ‘Disulfide-bond-induced
structural frustration and dynamic disorder in a peroxiredoxin from MAS NMR’,
Institute of Science and Technology Austria, 10.15479/AT:ISTA:12820.
mla: Schanda, Paul. Research Data of the Publication “Disulfide-Bond-Induced
Structural Frustration and Dynamic Disorder in a Peroxiredoxin from MAS NMR.”
Institute of Science and Technology Austria, 2023, doi:10.15479/AT:ISTA:12820.
short: P. Schanda, (2023).
contributor:
- contributor_type: researcher
first_name: Laura
last_name: Troussicot
- contributor_type: researcher
first_name: Björn M.
last_name: Burmann
date_created: 2023-04-10T05:55:56Z
date_published: 2023-04-18T00:00:00Z
date_updated: 2023-08-01T14:48:08Z
day: '18'
ddc:
- '570'
department:
- _id: PaSc
doi: 10.15479/AT:ISTA:12820
file:
- access_level: open_access
checksum: 54a619605e44c871214fb0e07b05c6bf
content_type: application/zip
creator: pschanda
date_created: 2023-04-14T09:39:33Z
date_updated: 2023-04-14T09:39:33Z
file_id: '12823'
file_name: data_deposition.zip
file_size: 54184807
relation: main_file
success: 1
- access_level: open_access
checksum: 8dede9fc78399d13144eb05c62bf5750
content_type: application/octet-stream
creator: pschanda
date_created: 2023-04-14T09:39:58Z
date_updated: 2023-04-14T09:39:58Z
file_id: '12824'
file_name: README
file_size: 4978
relation: main_file
success: 1
file_date_updated: 2023-04-14T09:39:58Z
has_accepted_license: '1'
month: '04'
oa: 1
oa_version: Published Version
publisher: Institute of Science and Technology Austria
related_material:
record:
- id: '13095'
relation: used_in_publication
status: public
status: public
title: Research data of the publication "Disulfide-bond-induced structural frustration
and dynamic disorder in a peroxiredoxin from MAS NMR"
tmp:
image: /images/cc_by_nc.png
legal_code_url: https://creativecommons.org/licenses/by-nc/4.0/legalcode
name: Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)
short: CC BY-NC (4.0)
type: research_data
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
year: '2023'
...
---
_id: '11179'
abstract:
- lang: eng
text: Large oligomeric enzymes control a myriad of cellular processes, from protein
synthesis and degradation to metabolism. The 0.5 MDa large TET2 aminopeptidase,
a prototypical protease important for cellular homeostasis, degrades peptides
within a ca. 60 Å wide tetrahedral chamber with four lateral openings. The mechanisms
of substrate trafficking and processing remain debated. Here, we integrate magic-angle
spinning (MAS) NMR, mutagenesis, co-evolution analysis and molecular dynamics
simulations and reveal that a loop in the catalytic chamber is a key element for
enzymatic function. The loop is able to stabilize ligands in the active site and
may additionally have a direct role in activating the catalytic water molecule
whereby a conserved histidine plays a key role. Our data provide a strong case
for the functional importance of highly dynamic - and often overlooked - parts
of an enzyme, and the potential of MAS NMR to investigate their dynamics at atomic
resolution.
acknowledgement: "We are grateful to Bernhard Brutscher, Alicia Vallet, and Adrien
Favier for excellent NMR\r\nplatform operation and management. The plasmid coding
for TET2 was kindly provided\r\nby Bruno Franzetti and Jerome Boisbouvier (IBS Grenoble).
We thank Anne-Marie Villard\r\nand the RoBioMol platform for preparing the loop
deletion construct. The RoBioMol\r\nplatform is part of the Grenoble Instruct-ERIC
center (ISBG; UAR 3518 CNRS-CEAUGA-EMBL) within the Grenoble Partnership for Structural
Biology (PSB), supported by FRISBI (ANR-10-INBS-0005-02) and GRAL (ANR-10-LABX-49-01),
financed within the University Grenoble Alpes graduate school (Ecoles Universitaires
de Recherche) CBHEUR-GS (ANR-17-EURE-0003). This work was supported by the European
Research Council (StG-2012-311318-ProtDyn2Function to P. S.) and the French Agence
Nationale de la Recherche (ANR), under grant ANR-14-ACHN-0016 (M.P. and A.B.)."
article_number: '1927'
article_processing_charge: No
article_type: original
author:
- first_name: Diego F.
full_name: Gauto, Diego F.
last_name: Gauto
- first_name: Pavel
full_name: Macek, Pavel
last_name: Macek
- first_name: Duccio
full_name: Malinverni, Duccio
last_name: Malinverni
- first_name: Hugo
full_name: Fraga, Hugo
last_name: Fraga
- first_name: Matteo
full_name: Paloni, Matteo
last_name: Paloni
- first_name: Iva
full_name: Sučec, Iva
last_name: Sučec
- first_name: Audrey
full_name: Hessel, Audrey
last_name: Hessel
- first_name: Juan Pablo
full_name: Bustamante, Juan Pablo
last_name: Bustamante
- first_name: Alessandro
full_name: Barducci, Alessandro
last_name: Barducci
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: Gauto DF, Macek P, Malinverni D, et al. Functional control of a 0.5 MDa TET
aminopeptidase by a flexible loop revealed by MAS NMR. Nature Communications.
2022;13. doi:10.1038/s41467-022-29423-0
apa: Gauto, D. F., Macek, P., Malinverni, D., Fraga, H., Paloni, M., Sučec, I.,
… Schanda, P. (2022). Functional control of a 0.5 MDa TET aminopeptidase by a
flexible loop revealed by MAS NMR. Nature Communications. Springer Nature.
https://doi.org/10.1038/s41467-022-29423-0
chicago: Gauto, Diego F., Pavel Macek, Duccio Malinverni, Hugo Fraga, Matteo Paloni,
Iva Sučec, Audrey Hessel, Juan Pablo Bustamante, Alessandro Barducci, and Paul
Schanda. “Functional Control of a 0.5 MDa TET Aminopeptidase by a Flexible Loop
Revealed by MAS NMR.” Nature Communications. Springer Nature, 2022. https://doi.org/10.1038/s41467-022-29423-0.
ieee: D. F. Gauto et al., “Functional control of a 0.5 MDa TET aminopeptidase
by a flexible loop revealed by MAS NMR,” Nature Communications, vol. 13.
Springer Nature, 2022.
ista: Gauto DF, Macek P, Malinverni D, Fraga H, Paloni M, Sučec I, Hessel A, Bustamante
JP, Barducci A, Schanda P. 2022. Functional control of a 0.5 MDa TET aminopeptidase
by a flexible loop revealed by MAS NMR. Nature Communications. 13, 1927.
mla: Gauto, Diego F., et al. “Functional Control of a 0.5 MDa TET Aminopeptidase
by a Flexible Loop Revealed by MAS NMR.” Nature Communications, vol. 13,
1927, Springer Nature, 2022, doi:10.1038/s41467-022-29423-0.
short: D.F. Gauto, P. Macek, D. Malinverni, H. Fraga, M. Paloni, I. Sučec, A. Hessel,
J.P. Bustamante, A. Barducci, P. Schanda, Nature Communications 13 (2022).
date_created: 2022-04-17T22:01:45Z
date_published: 2022-04-08T00:00:00Z
date_updated: 2023-08-03T06:54:56Z
day: '08'
ddc:
- '570'
department:
- _id: PaSc
doi: 10.1038/s41467-022-29423-0
external_id:
isi:
- '000781498700009'
file:
- access_level: open_access
checksum: db61d5534e988743d6266d3675d77b08
content_type: application/pdf
creator: dernst
date_created: 2022-05-02T08:48:00Z
date_updated: 2022-05-02T08:48:00Z
file_id: '11348'
file_name: 2022_NatureCommunications_Gauto.pdf
file_size: 2637590
relation: main_file
success: 1
file_date_updated: 2022-05-02T08:48:00Z
has_accepted_license: '1'
intvolume: ' 13'
isi: 1
language:
- iso: eng
month: '04'
oa: 1
oa_version: Published Version
publication: Nature Communications
publication_identifier:
eissn:
- 2041-1723
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
related_material:
link:
- relation: erratum
url: https://doi.org/10.1038/s41467-022-31243-1
scopus_import: '1'
status: public
title: Functional control of a 0.5 MDa TET aminopeptidase by a flexible loop revealed
by MAS NMR
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 13
year: '2022'
...
---
_id: '10323'
abstract:
- lang: eng
text: Molecular chaperones are central to cellular protein homeostasis. Dynamic
disorder is a key feature of the complexes of molecular chaperones and their client
proteins, and it facilitates the client release towards a folded state or the
handover to downstream components. The dynamic nature also implies that a given
chaperone can interact with many different client proteins, based on physico-chemical
sequence properties rather than on structural complementarity of their (folded)
3D structure. Yet, the balance between this promiscuity and some degree of client
specificity is poorly understood. Here, we review recent atomic-level descriptions
of chaperones with client proteins, including chaperones in complex with intrinsically
disordered proteins, with membrane-protein precursors, or partially folded client
proteins. We focus hereby on chaperone-client interactions that are independent
of ATP. The picture emerging from these studies highlights the importance of dynamics
in these complexes, whereby several interaction types, not only hydrophobic ones,
contribute to the complex formation. We discuss these features of chaperone-client
complexes and possible factors that may contribute to this balance of promiscuity
and specificity.
acknowledgement: We thank Juan C. Fontecilla-Camps for insightful discussions related
to ATP-driven machineries, and Elif Karagöz for providing the structural model of
the Hsp90-Tau complex. This study was supported by the European Research Council
(StG-2012-311318-ProtDyn2Function) and the Agence Nationale de la Recherche (ANR-18-CE92-0032-MitoMemProtImp).
article_number: '762005'
article_processing_charge: Yes (via OA deal)
article_type: original
author:
- first_name: Iva
full_name: Sučec, Iva
last_name: Sučec
- first_name: Beate
full_name: Bersch, Beate
last_name: Bersch
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: Sučec I, Bersch B, Schanda P. How do chaperones bind (partly) unfolded client
proteins? Frontiers in Molecular Biosciences. 2021;8. doi:10.3389/fmolb.2021.762005
apa: Sučec, I., Bersch, B., & Schanda, P. (2021). How do chaperones bind (partly)
unfolded client proteins? Frontiers in Molecular Biosciences. Frontiers.
https://doi.org/10.3389/fmolb.2021.762005
chicago: Sučec, Iva, Beate Bersch, and Paul Schanda. “How Do Chaperones Bind (Partly)
Unfolded Client Proteins?” Frontiers in Molecular Biosciences. Frontiers,
2021. https://doi.org/10.3389/fmolb.2021.762005.
ieee: I. Sučec, B. Bersch, and P. Schanda, “How do chaperones bind (partly) unfolded
client proteins?,” Frontiers in Molecular Biosciences, vol. 8. Frontiers,
2021.
ista: Sučec I, Bersch B, Schanda P. 2021. How do chaperones bind (partly) unfolded
client proteins? Frontiers in Molecular Biosciences. 8, 762005.
mla: Sučec, Iva, et al. “How Do Chaperones Bind (Partly) Unfolded Client Proteins?”
Frontiers in Molecular Biosciences, vol. 8, 762005, Frontiers, 2021, doi:10.3389/fmolb.2021.762005.
short: I. Sučec, B. Bersch, P. Schanda, Frontiers in Molecular Biosciences 8 (2021).
date_created: 2021-11-21T23:01:29Z
date_published: 2021-10-25T00:00:00Z
date_updated: 2023-08-14T11:55:04Z
day: '25'
ddc:
- '547'
department:
- _id: PaSc
doi: 10.3389/fmolb.2021.762005
external_id:
isi:
- '000717241700001'
pmid:
- '34760928'
file:
- access_level: open_access
checksum: a5c9dbf80dc2c5aaa737f456c941d964
content_type: application/pdf
creator: cchlebak
date_created: 2021-11-23T15:06:58Z
date_updated: 2021-11-23T15:06:58Z
file_id: '10333'
file_name: 2021_FrontiersMolBioSc_Sučec.pdf
file_size: 4700798
relation: main_file
success: 1
file_date_updated: 2021-11-23T15:06:58Z
has_accepted_license: '1'
intvolume: ' 8'
isi: 1
language:
- iso: eng
month: '10'
oa: 1
oa_version: Published Version
pmid: 1
publication: Frontiers in Molecular Biosciences
publication_identifier:
eissn:
- 2296-889X
publication_status: published
publisher: Frontiers
quality_controlled: '1'
scopus_import: '1'
status: public
title: How do chaperones bind (partly) unfolded client proteins?
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 8
year: '2021'
...
---
_id: '8402'
abstract:
- lang: eng
text: "Background: The mitochondrial pyruvate carrier (MPC) plays a central role
in energy metabolism by transporting pyruvate across the inner mitochondrial membrane.
Its heterodimeric composition and homology to SWEET and semiSWEET transporters
set the MPC apart from the canonical mitochondrial carrier family (named MCF or
SLC25). The import of the canonical carriers is mediated by the carrier translocase
of the inner membrane (TIM22) pathway and is dependent on their structure, which
features an even number of transmembrane segments and both termini in the intermembrane
space. The import pathway of MPC proteins has not been elucidated. The odd number
of transmembrane segments and positioning of the N-terminus in the matrix argues
against an import via the TIM22 carrier pathway but favors an import via the flexible
presequence pathway.\r\nResults: Here, we systematically analyzed the import pathways
of Mpc2 and Mpc3 and report that, contrary to an expected import via the flexible
presequence pathway, yeast MPC proteins with an odd number of transmembrane segments
and matrix-exposed N-terminus are imported by the carrier pathway, using the receptor
Tom70, small TIM chaperones, and the TIM22 complex. The TIM9·10 complex chaperones
MPC proteins through the mitochondrial intermembrane space using conserved hydrophobic
motifs that are also required for the interaction with canonical carrier proteins.\r\nConclusions:
The carrier pathway can import paired and non-paired transmembrane helices and
translocate N-termini to either side of the mitochondrial inner membrane, revealing
an unexpected versatility of the mitochondrial import pathway for non-cleavable
inner membrane proteins."
article_number: '2'
article_processing_charge: No
article_type: original
author:
- first_name: Heike
full_name: Rampelt, Heike
last_name: Rampelt
- first_name: Iva
full_name: Sucec, Iva
last_name: Sucec
- first_name: Beate
full_name: Bersch, Beate
last_name: Bersch
- first_name: Patrick
full_name: Horten, Patrick
last_name: Horten
- first_name: Inge
full_name: Perschil, Inge
last_name: Perschil
- first_name: Jean-Claude
full_name: Martinou, Jean-Claude
last_name: Martinou
- first_name: Martin
full_name: van der Laan, Martin
last_name: van der Laan
- first_name: Nils
full_name: Wiedemann, Nils
last_name: Wiedemann
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Nikolaus
full_name: Pfanner, Nikolaus
last_name: Pfanner
citation:
ama: Rampelt H, Sucec I, Bersch B, et al. The mitochondrial carrier pathway transports
non-canonical substrates with an odd number of transmembrane segments. BMC
Biology. 2020;18. doi:10.1186/s12915-019-0733-6
apa: Rampelt, H., Sucec, I., Bersch, B., Horten, P., Perschil, I., Martinou, J.-C.,
… Pfanner, N. (2020). The mitochondrial carrier pathway transports non-canonical
substrates with an odd number of transmembrane segments. BMC Biology. Springer
Nature. https://doi.org/10.1186/s12915-019-0733-6
chicago: Rampelt, Heike, Iva Sucec, Beate Bersch, Patrick Horten, Inge Perschil,
Jean-Claude Martinou, Martin van der Laan, Nils Wiedemann, Paul Schanda, and Nikolaus
Pfanner. “The Mitochondrial Carrier Pathway Transports Non-Canonical Substrates
with an Odd Number of Transmembrane Segments.” BMC Biology. Springer Nature,
2020. https://doi.org/10.1186/s12915-019-0733-6.
ieee: H. Rampelt et al., “The mitochondrial carrier pathway transports non-canonical
substrates with an odd number of transmembrane segments,” BMC Biology,
vol. 18. Springer Nature, 2020.
ista: Rampelt H, Sucec I, Bersch B, Horten P, Perschil I, Martinou J-C, van der
Laan M, Wiedemann N, Schanda P, Pfanner N. 2020. The mitochondrial carrier pathway
transports non-canonical substrates with an odd number of transmembrane segments.
BMC Biology. 18, 2.
mla: Rampelt, Heike, et al. “The Mitochondrial Carrier Pathway Transports Non-Canonical
Substrates with an Odd Number of Transmembrane Segments.” BMC Biology,
vol. 18, 2, Springer Nature, 2020, doi:10.1186/s12915-019-0733-6.
short: H. Rampelt, I. Sucec, B. Bersch, P. Horten, I. Perschil, J.-C. Martinou,
M. van der Laan, N. Wiedemann, P. Schanda, N. Pfanner, BMC Biology 18 (2020).
date_created: 2020-09-17T10:26:53Z
date_published: 2020-01-06T00:00:00Z
date_updated: 2021-01-12T08:19:02Z
day: '06'
doi: 10.1186/s12915-019-0733-6
extern: '1'
external_id:
pmid:
- '31907035'
intvolume: ' 18'
keyword:
- Biotechnology
- Plant Science
- General Biochemistry
- Genetics and Molecular Biology
- Developmental Biology
- Cell Biology
- Physiology
- Ecology
- Evolution
- Behavior and Systematics
- Structural Biology
- General Agricultural and Biological Sciences
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1186/s12915-019-0733-6
month: '01'
oa: 1
oa_version: Published Version
pmid: 1
publication: BMC Biology
publication_identifier:
issn:
- 1741-7007
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
status: public
title: The mitochondrial carrier pathway transports non-canonical substrates with
an odd number of transmembrane segments
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 18
year: '2020'
...
---
_id: '8403'
abstract:
- lang: eng
text: Chaperones are essential for assisting protein folding, and for transferring
poorly soluble proteins to their functional locations within cells. Hydrophobic
interactions drive promiscuous chaperone–client binding, but our understanding
of how additional interactions enable client specificity is sparse. Here we decipher
what determines binding of two chaperones (TIM8·13, TIM9·10) to different integral
membrane proteins, the all-transmembrane mitochondrial carrier Ggc1, and Tim23
which has an additional disordered hydrophilic domain. Combining NMR, SAXS and
molecular dynamics simulations, we determine the structures of Tim23/TIM8·13 and
Tim23/TIM9·10 complexes. TIM8·13 uses transient salt bridges to interact with
the hydrophilic part of its client, but its interactions to the transmembrane
part are weaker than in TIM9·10. Consequently, TIM9·10 outcompetes TIM8·13 in
binding hydrophobic clients, while TIM8·13 is tuned to few clients with both hydrophilic
and hydrophobic parts. Our study exemplifies how chaperones fine-tune the balance
of promiscuity vs. specificity.
article_processing_charge: No
author:
- first_name: Iva
full_name: Sučec, Iva
last_name: Sučec
- first_name: Yong
full_name: Wang, Yong
last_name: Wang
- first_name: Ons
full_name: Dakhlaoui, Ons
last_name: Dakhlaoui
- first_name: Katharina
full_name: Weinhäupl, Katharina
last_name: Weinhäupl
- first_name: Tobias
full_name: Jores, Tobias
last_name: Jores
- first_name: Doriane
full_name: Costa, Doriane
last_name: Costa
- first_name: Audrey
full_name: Hessel, Audrey
last_name: Hessel
- first_name: Martha
full_name: Brennich, Martha
last_name: Brennich
- first_name: Doron
full_name: Rapaport, Doron
last_name: Rapaport
- first_name: Kresten
full_name: Lindorff-Larsen, Kresten
last_name: Lindorff-Larsen
- first_name: Beate
full_name: Bersch, Beate
last_name: Bersch
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: Sučec I, Wang Y, Dakhlaoui O, et al. Structural basis of client specificity
in mitochondrial membrane-protein chaperones. bioRxiv. doi:10.1101/2020.06.08.140772
apa: Sučec, I., Wang, Y., Dakhlaoui, O., Weinhäupl, K., Jores, T., Costa, D., …
Schanda, P. (n.d.). Structural basis of client specificity in mitochondrial membrane-protein
chaperones. bioRxiv. Cold Spring Harbor Laboratory. https://doi.org/10.1101/2020.06.08.140772
chicago: Sučec, Iva, Yong Wang, Ons Dakhlaoui, Katharina Weinhäupl, Tobias Jores,
Doriane Costa, Audrey Hessel, et al. “Structural Basis of Client Specificity in
Mitochondrial Membrane-Protein Chaperones.” BioRxiv. Cold Spring Harbor
Laboratory, n.d. https://doi.org/10.1101/2020.06.08.140772.
ieee: I. Sučec et al., “Structural basis of client specificity in mitochondrial
membrane-protein chaperones,” bioRxiv. Cold Spring Harbor Laboratory.
ista: Sučec I, Wang Y, Dakhlaoui O, Weinhäupl K, Jores T, Costa D, Hessel A, Brennich
M, Rapaport D, Lindorff-Larsen K, Bersch B, Schanda P. Structural basis of client
specificity in mitochondrial membrane-protein chaperones. bioRxiv, 10.1101/2020.06.08.140772.
mla: Sučec, Iva, et al. “Structural Basis of Client Specificity in Mitochondrial
Membrane-Protein Chaperones.” BioRxiv, Cold Spring Harbor Laboratory, doi:10.1101/2020.06.08.140772.
short: I. Sučec, Y. Wang, O. Dakhlaoui, K. Weinhäupl, T. Jores, D. Costa, A. Hessel,
M. Brennich, D. Rapaport, K. Lindorff-Larsen, B. Bersch, P. Schanda, BioRxiv (n.d.).
date_created: 2020-09-17T10:27:47Z
date_published: 2020-09-17T00:00:00Z
date_updated: 2021-01-12T08:19:02Z
day: '17'
doi: 10.1101/2020.06.08.140772
extern: '1'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1101/2020.06.08.140772
month: '09'
oa: 1
oa_version: Preprint
publication: bioRxiv
publication_status: submitted
publisher: Cold Spring Harbor Laboratory
status: public
title: Structural basis of client specificity in mitochondrial membrane-protein chaperones
type: preprint
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
year: '2020'
...
---
_id: '8404'
abstract:
- lang: eng
text: The mitochondrial Tim chaperones are responsible for the transport
of membrane proteins across the inter-membrane space to the inner and outer mitochondrial
membranes. TIM9·10, a hexameric 70 kDa protein complex formed by 3 copies of Tim9
and Tim10, guides its clients across the aqueous compartment. The TIM9·10·12 complex
is the anchor point at the inner-membrane insertase complex TIM22. The mechanism
of client transport by TIM9·10 has been resolved recently, but the structure and
subunit composition of the TIM9·10·12 complex remains largely unresolved. Furthermore,
the assembly process of the hexameric TIM chaperones from its subunits remained
elusive. We investigate the structural and dynamical properties of the Tim subunits,
and show that they are highly dynamic. In their non-assembled form, the subunits
behave as intrinsically disordered proteins; when the conserved cysteines of the
CX3C-Xn-CX3C
motifs are formed, short marginally stable α-helices
are formed, which are only fully stabilized upon hexamer formation to the mature
chaperone. Subunits are in equilibrium between their hexamer-embedded and a free
form, with exchange kinetics on a minutes time scale. Joint NMR, small-angle X-ray
scattering and MD simulation data allow us to derive a structural model of the
TIM9·10·12 assembly, which has a 2:3:1 stoichiometry (Tim9:Tim10:Tim12) with a
conserved hydrophobic client-binding groove and flexible N- and C-terminal tentacles.
article_processing_charge: No
author:
- first_name: Katharina
full_name: Weinhäupl, Katharina
last_name: Weinhäupl
- first_name: Yong
full_name: Wang, Yong
last_name: Wang
- first_name: Audrey
full_name: Hessel, Audrey
last_name: Hessel
- first_name: Martha
full_name: Brennich, Martha
last_name: Brennich
- first_name: Kresten
full_name: Lindorff-Larsen, Kresten
last_name: Lindorff-Larsen
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: Weinhäupl K, Wang Y, Hessel A, Brennich M, Lindorff-Larsen K, Schanda P. Architecture
and subunit dynamics of the mitochondrial TIM9·10·12 chaperone. bioRxiv.
doi:10.1101/2020.03.13.990150
apa: Weinhäupl, K., Wang, Y., Hessel, A., Brennich, M., Lindorff-Larsen, K., &
Schanda, P. (n.d.). Architecture and subunit dynamics of the mitochondrial TIM9·10·12
chaperone. bioRxiv. Cold Spring Harbor Laboratory. https://doi.org/10.1101/2020.03.13.990150
chicago: Weinhäupl, Katharina, Yong Wang, Audrey Hessel, Martha Brennich, Kresten
Lindorff-Larsen, and Paul Schanda. “Architecture and Subunit Dynamics of the Mitochondrial
TIM9·10·12 Chaperone.” BioRxiv. Cold Spring Harbor Laboratory, n.d. https://doi.org/10.1101/2020.03.13.990150.
ieee: K. Weinhäupl, Y. Wang, A. Hessel, M. Brennich, K. Lindorff-Larsen, and P.
Schanda, “Architecture and subunit dynamics of the mitochondrial TIM9·10·12 chaperone,”
bioRxiv. Cold Spring Harbor Laboratory.
ista: Weinhäupl K, Wang Y, Hessel A, Brennich M, Lindorff-Larsen K, Schanda P. Architecture
and subunit dynamics of the mitochondrial TIM9·10·12 chaperone. bioRxiv, 10.1101/2020.03.13.990150.
mla: Weinhäupl, Katharina, et al. “Architecture and Subunit Dynamics of the Mitochondrial
TIM9·10·12 Chaperone.” BioRxiv, Cold Spring Harbor Laboratory, doi:10.1101/2020.03.13.990150.
short: K. Weinhäupl, Y. Wang, A. Hessel, M. Brennich, K. Lindorff-Larsen, P. Schanda,
BioRxiv (n.d.).
date_created: 2020-09-17T10:27:59Z
date_published: 2020-03-14T00:00:00Z
date_updated: 2021-01-12T08:19:03Z
day: '14'
doi: 10.1101/2020.03.13.990150
extern: '1'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1101/2020.03.13.990150
month: '03'
oa: 1
oa_version: Preprint
publication: bioRxiv
publication_status: submitted
publisher: Cold Spring Harbor Laboratory
status: public
title: Architecture and subunit dynamics of the mitochondrial TIM9·10·12 chaperone
type: preprint
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
year: '2020'
...
---
_id: '8405'
abstract:
- lang: eng
text: Atomic-resolution structure determination is crucial for understanding protein
function. Cryo-EM and NMR spectroscopy both provide structural information, but
currently cryo-EM does not routinely give access to atomic-level structural data,
and, generally, NMR structure determination is restricted to small (<30 kDa) proteins.
We introduce an integrated structure determination approach that simultaneously
uses NMR and EM data to overcome the limits of each of these methods. The approach
enables structure determination of the 468 kDa large dodecameric aminopeptidase
TET2 to a precision and accuracy below 1 Å by combining secondary-structure information
obtained from near-complete magic-angle-spinning NMR assignments of the 39 kDa-large
subunits, distance restraints from backbone amides and ILV methyl groups, and
a 4.1 Å resolution EM map. The resulting structure exceeds current standards of
NMR and EM structure determination in terms of molecular weight and precision.
Importantly, the approach is successful even in cases where only medium-resolution
cryo-EM data are available.
article_number: '2697'
article_processing_charge: No
article_type: original
author:
- first_name: Diego F.
full_name: Gauto, Diego F.
last_name: Gauto
- first_name: Leandro F.
full_name: Estrozi, Leandro F.
last_name: Estrozi
- first_name: Charles D.
full_name: Schwieters, Charles D.
last_name: Schwieters
- first_name: Gregory
full_name: Effantin, Gregory
last_name: Effantin
- first_name: Pavel
full_name: Macek, Pavel
last_name: Macek
- first_name: Remy
full_name: Sounier, Remy
last_name: Sounier
- first_name: Astrid C.
full_name: Sivertsen, Astrid C.
last_name: Sivertsen
- first_name: Elena
full_name: Schmidt, Elena
last_name: Schmidt
- first_name: Rime
full_name: Kerfah, Rime
last_name: Kerfah
- first_name: Guillaume
full_name: Mas, Guillaume
last_name: Mas
- first_name: Jacques-Philippe
full_name: Colletier, Jacques-Philippe
last_name: Colletier
- first_name: Peter
full_name: Güntert, Peter
last_name: Güntert
- first_name: Adrien
full_name: Favier, Adrien
last_name: Favier
- first_name: Guy
full_name: Schoehn, Guy
last_name: Schoehn
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Jerome
full_name: Boisbouvier, Jerome
last_name: Boisbouvier
citation:
ama: Gauto DF, Estrozi LF, Schwieters CD, et al. Integrated NMR and cryo-EM atomic-resolution
structure determination of a half-megadalton enzyme complex. Nature Communications.
2019;10. doi:10.1038/s41467-019-10490-9
apa: Gauto, D. F., Estrozi, L. F., Schwieters, C. D., Effantin, G., Macek, P., Sounier,
R., … Boisbouvier, J. (2019). Integrated NMR and cryo-EM atomic-resolution structure
determination of a half-megadalton enzyme complex. Nature Communications.
Springer Nature. https://doi.org/10.1038/s41467-019-10490-9
chicago: Gauto, Diego F., Leandro F. Estrozi, Charles D. Schwieters, Gregory Effantin,
Pavel Macek, Remy Sounier, Astrid C. Sivertsen, et al. “Integrated NMR and Cryo-EM
Atomic-Resolution Structure Determination of a Half-Megadalton Enzyme Complex.”
Nature Communications. Springer Nature, 2019. https://doi.org/10.1038/s41467-019-10490-9.
ieee: D. F. Gauto et al., “Integrated NMR and cryo-EM atomic-resolution structure
determination of a half-megadalton enzyme complex,” Nature Communications,
vol. 10. Springer Nature, 2019.
ista: Gauto DF, Estrozi LF, Schwieters CD, Effantin G, Macek P, Sounier R, Sivertsen
AC, Schmidt E, Kerfah R, Mas G, Colletier J-P, Güntert P, Favier A, Schoehn G,
Schanda P, Boisbouvier J. 2019. Integrated NMR and cryo-EM atomic-resolution structure
determination of a half-megadalton enzyme complex. Nature Communications. 10,
2697.
mla: Gauto, Diego F., et al. “Integrated NMR and Cryo-EM Atomic-Resolution Structure
Determination of a Half-Megadalton Enzyme Complex.” Nature Communications,
vol. 10, 2697, Springer Nature, 2019, doi:10.1038/s41467-019-10490-9.
short: D.F. Gauto, L.F. Estrozi, C.D. Schwieters, G. Effantin, P. Macek, R. Sounier,
A.C. Sivertsen, E. Schmidt, R. Kerfah, G. Mas, J.-P. Colletier, P. Güntert, A.
Favier, G. Schoehn, P. Schanda, J. Boisbouvier, Nature Communications 10 (2019).
date_created: 2020-09-17T10:28:25Z
date_published: 2019-06-19T00:00:00Z
date_updated: 2021-01-12T08:19:03Z
day: '19'
doi: 10.1038/s41467-019-10490-9
extern: '1'
external_id:
pmid:
- '31217444'
intvolume: ' 10'
keyword:
- General Biochemistry
- Genetics and Molecular Biology
- General Physics and Astronomy
- General Chemistry
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1038/s41467-019-10490-9
month: '06'
oa: 1
oa_version: Published Version
pmid: 1
publication: Nature Communications
publication_identifier:
issn:
- 2041-1723
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
status: public
title: Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton
enzyme complex
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 10
year: '2019'
...
---
_id: '8406'
abstract:
- lang: eng
text: Coordinated conformational transitions in oligomeric enzymatic complexes modulate
function in response to substrates and play a crucial role in enzyme inhibition
and activation. Caseinolytic protease (ClpP) is a tetradecameric complex, which
has emerged as a drug target against multiple pathogenic bacteria. Activation
of different ClpPs by inhibitors has been independently reported from drug development
efforts, but no rationale for inhibitor-induced activation has been hitherto proposed.
Using an integrated approach that includes x-ray crystallography, solid- and solution-state
nuclear magnetic resonance, molecular dynamics simulations, and isothermal titration
calorimetry, we show that the proteasome inhibitor bortezomib binds to the ClpP
active-site serine, mimicking a peptide substrate, and induces a concerted allosteric
activation of the complex. The bortezomib-activated conformation also exhibits
a higher affinity for its cognate unfoldase ClpX. We propose a universal allosteric
mechanism, where substrate binding to a single subunit locks ClpP into an active
conformation optimized for chaperone association and protein processive degradation.
article_number: eaaw3818
article_processing_charge: No
article_type: original
author:
- first_name: Jan
full_name: Felix, Jan
last_name: Felix
- first_name: Katharina
full_name: Weinhäupl, Katharina
last_name: Weinhäupl
- first_name: Christophe
full_name: Chipot, Christophe
last_name: Chipot
- first_name: François
full_name: Dehez, François
last_name: Dehez
- first_name: Audrey
full_name: Hessel, Audrey
last_name: Hessel
- first_name: Diego F.
full_name: Gauto, Diego F.
last_name: Gauto
- first_name: Cecile
full_name: Morlot, Cecile
last_name: Morlot
- first_name: Olga
full_name: Abian, Olga
last_name: Abian
- first_name: Irina
full_name: Gutsche, Irina
last_name: Gutsche
- first_name: Adrian
full_name: Velazquez-Campoy, Adrian
last_name: Velazquez-Campoy
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Hugo
full_name: Fraga, Hugo
last_name: Fraga
citation:
ama: Felix J, Weinhäupl K, Chipot C, et al. Mechanism of the allosteric activation
of the ClpP protease machinery by substrates and active-site inhibitors. Science
Advances. 2019;5(9). doi:10.1126/sciadv.aaw3818
apa: Felix, J., Weinhäupl, K., Chipot, C., Dehez, F., Hessel, A., Gauto, D. F.,
… Fraga, H. (2019). Mechanism of the allosteric activation of the ClpP protease
machinery by substrates and active-site inhibitors. Science Advances. American
Association for the Advancement of Science. https://doi.org/10.1126/sciadv.aaw3818
chicago: Felix, Jan, Katharina Weinhäupl, Christophe Chipot, François Dehez, Audrey
Hessel, Diego F. Gauto, Cecile Morlot, et al. “Mechanism of the Allosteric Activation
of the ClpP Protease Machinery by Substrates and Active-Site Inhibitors.” Science
Advances. American Association for the Advancement of Science, 2019. https://doi.org/10.1126/sciadv.aaw3818.
ieee: J. Felix et al., “Mechanism of the allosteric activation of the ClpP
protease machinery by substrates and active-site inhibitors,” Science Advances,
vol. 5, no. 9. American Association for the Advancement of Science, 2019.
ista: Felix J, Weinhäupl K, Chipot C, Dehez F, Hessel A, Gauto DF, Morlot C, Abian
O, Gutsche I, Velazquez-Campoy A, Schanda P, Fraga H. 2019. Mechanism of the allosteric
activation of the ClpP protease machinery by substrates and active-site inhibitors.
Science Advances. 5(9), eaaw3818.
mla: Felix, Jan, et al. “Mechanism of the Allosteric Activation of the ClpP Protease
Machinery by Substrates and Active-Site Inhibitors.” Science Advances,
vol. 5, no. 9, eaaw3818, American Association for the Advancement of Science,
2019, doi:10.1126/sciadv.aaw3818.
short: J. Felix, K. Weinhäupl, C. Chipot, F. Dehez, A. Hessel, D.F. Gauto, C. Morlot,
O. Abian, I. Gutsche, A. Velazquez-Campoy, P. Schanda, H. Fraga, Science Advances
5 (2019).
date_created: 2020-09-17T10:28:36Z
date_published: 2019-09-04T00:00:00Z
date_updated: 2021-01-12T08:19:03Z
day: '04'
doi: 10.1126/sciadv.aaw3818
extern: '1'
intvolume: ' 5'
issue: '9'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: ' https://doi.org/10.1126/sciadv.aaw3818'
month: '09'
oa: 1
oa_version: Published Version
publication: Science Advances
publication_identifier:
issn:
- 2375-2548
publication_status: published
publisher: American Association for the Advancement of Science
quality_controlled: '1'
status: public
title: Mechanism of the allosteric activation of the ClpP protease machinery by substrates
and active-site inhibitors
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 5
year: '2019'
...
---
_id: '8407'
article_processing_charge: No
article_type: original
author:
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: Schanda P. Relaxing with liquids and solids – A perspective on biomolecular
dynamics. Journal of Magnetic Resonance. 2019;306:180-186. doi:10.1016/j.jmr.2019.07.025
apa: Schanda, P. (2019). Relaxing with liquids and solids – A perspective on biomolecular
dynamics. Journal of Magnetic Resonance. Elsevier. https://doi.org/10.1016/j.jmr.2019.07.025
chicago: Schanda, Paul. “Relaxing with Liquids and Solids – A Perspective on Biomolecular
Dynamics.” Journal of Magnetic Resonance. Elsevier, 2019. https://doi.org/10.1016/j.jmr.2019.07.025.
ieee: P. Schanda, “Relaxing with liquids and solids – A perspective on biomolecular
dynamics,” Journal of Magnetic Resonance, vol. 306. Elsevier, pp. 180–186,
2019.
ista: Schanda P. 2019. Relaxing with liquids and solids – A perspective on biomolecular
dynamics. Journal of Magnetic Resonance. 306, 180–186.
mla: Schanda, Paul. “Relaxing with Liquids and Solids – A Perspective on Biomolecular
Dynamics.” Journal of Magnetic Resonance, vol. 306, Elsevier, 2019, pp.
180–86, doi:10.1016/j.jmr.2019.07.025.
short: P. Schanda, Journal of Magnetic Resonance 306 (2019) 180–186.
date_created: 2020-09-17T10:28:47Z
date_published: 2019-09-01T00:00:00Z
date_updated: 2021-01-12T08:19:04Z
day: '01'
doi: 10.1016/j.jmr.2019.07.025
extern: '1'
external_id:
pmid:
- '31350165'
intvolume: ' 306'
keyword:
- Nuclear and High Energy Physics
- Biophysics
- Biochemistry
- Condensed Matter Physics
language:
- iso: eng
month: '09'
oa_version: Submitted Version
page: 180-186
pmid: 1
publication: Journal of Magnetic Resonance
publication_identifier:
issn:
- 1090-7807
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: Relaxing with liquids and solids – A perspective on biomolecular dynamics
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 306
year: '2019'
...
---
_id: '8408'
abstract:
- lang: eng
text: Aromatic residues are located at structurally important sites of many proteins.
Probing their interactions and dynamics can provide important functional insight
but is challenging in large proteins. Here, we introduce approaches to characterize
dynamics of phenylalanine residues using 1H-detected fast magic-angle spinning
(MAS) NMR combined with a tailored isotope-labeling scheme. Our approach yields
isolated two-spin systems that are ideally suited for artefact-free dynamics measurements,
and allows probing motions effectively without molecular-weight limitations. The
application to the TET2 enzyme assembly of ~0.5 MDa size, the currently largest
protein assigned by MAS NMR, provides insights into motions occurring on a wide
range of time scales (ps-ms). We quantitatively probe ring flip motions, and show
the temperature dependence by MAS NMR measurements down to 100 K. Interestingly,
favorable line widths are observed down to 100 K, with potential implications
for DNP NMR. Furthermore, we report the first 13C R1ρ MAS NMR relaxation-dispersion
measurements and detect structural excursions occurring on a microsecond time
scale in the entry pore to the catalytic chamber and at a trimer interface that
was proposed as exit pore. We show that the labeling scheme with deuteration at
ca. 50 kHz MAS provides superior resolution compared to 100 kHz MAS experiments
with protonated, uniformly 13C-labeled samples.
article_processing_charge: No
article_type: original
author:
- first_name: Diego F.
full_name: Gauto, Diego F.
last_name: Gauto
- first_name: Pavel
full_name: Macek, Pavel
last_name: Macek
- first_name: Alessandro
full_name: Barducci, Alessandro
last_name: Barducci
- first_name: Hugo
full_name: Fraga, Hugo
last_name: Fraga
- first_name: Audrey
full_name: Hessel, Audrey
last_name: Hessel
- first_name: Tsutomu
full_name: Terauchi, Tsutomu
last_name: Terauchi
- first_name: David
full_name: Gajan, David
last_name: Gajan
- first_name: Yohei
full_name: Miyanoiri, Yohei
last_name: Miyanoiri
- first_name: Jerome
full_name: Boisbouvier, Jerome
last_name: Boisbouvier
- first_name: Roman
full_name: Lichtenecker, Roman
last_name: Lichtenecker
- first_name: Masatsune
full_name: Kainosho, Masatsune
last_name: Kainosho
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: Gauto DF, Macek P, Barducci A, et al. Aromatic ring dynamics, thermal activation,
and transient conformations of a 468 kDa enzyme by specific 1H–13C labeling and
fast magic-angle spinning NMR. Journal of the American Chemical Society.
2019;141(28):11183-11195. doi:10.1021/jacs.9b04219
apa: Gauto, D. F., Macek, P., Barducci, A., Fraga, H., Hessel, A., Terauchi, T.,
… Schanda, P. (2019). Aromatic ring dynamics, thermal activation, and transient
conformations of a 468 kDa enzyme by specific 1H–13C labeling and fast magic-angle
spinning NMR. Journal of the American Chemical Society. American Chemical
Society. https://doi.org/10.1021/jacs.9b04219
chicago: Gauto, Diego F., Pavel Macek, Alessandro Barducci, Hugo Fraga, Audrey Hessel,
Tsutomu Terauchi, David Gajan, et al. “Aromatic Ring Dynamics, Thermal Activation,
and Transient Conformations of a 468 KDa Enzyme by Specific 1H–13C Labeling and
Fast Magic-Angle Spinning NMR.” Journal of the American Chemical Society.
American Chemical Society, 2019. https://doi.org/10.1021/jacs.9b04219.
ieee: D. F. Gauto et al., “Aromatic ring dynamics, thermal activation, and
transient conformations of a 468 kDa enzyme by specific 1H–13C labeling and fast
magic-angle spinning NMR,” Journal of the American Chemical Society, vol.
141, no. 28. American Chemical Society, pp. 11183–11195, 2019.
ista: Gauto DF, Macek P, Barducci A, Fraga H, Hessel A, Terauchi T, Gajan D, Miyanoiri
Y, Boisbouvier J, Lichtenecker R, Kainosho M, Schanda P. 2019. Aromatic ring dynamics,
thermal activation, and transient conformations of a 468 kDa enzyme by specific
1H–13C labeling and fast magic-angle spinning NMR. Journal of the American Chemical
Society. 141(28), 11183–11195.
mla: Gauto, Diego F., et al. “Aromatic Ring Dynamics, Thermal Activation, and Transient
Conformations of a 468 KDa Enzyme by Specific 1H–13C Labeling and Fast Magic-Angle
Spinning NMR.” Journal of the American Chemical Society, vol. 141, no.
28, American Chemical Society, 2019, pp. 11183–95, doi:10.1021/jacs.9b04219.
short: D.F. Gauto, P. Macek, A. Barducci, H. Fraga, A. Hessel, T. Terauchi, D. Gajan,
Y. Miyanoiri, J. Boisbouvier, R. Lichtenecker, M. Kainosho, P. Schanda, Journal
of the American Chemical Society 141 (2019) 11183–11195.
date_created: 2020-09-17T10:29:00Z
date_published: 2019-06-14T00:00:00Z
date_updated: 2021-01-12T08:19:04Z
day: '14'
doi: 10.1021/jacs.9b04219
extern: '1'
external_id:
pmid:
- '31199882'
intvolume: ' 141'
issue: '28'
keyword:
- Colloid and Surface Chemistry
- Biochemistry
- General Chemistry
- Catalysis
language:
- iso: eng
month: '06'
oa_version: Submitted Version
page: 11183-11195
pmid: 1
publication: Journal of the American Chemical Society
publication_identifier:
issn:
- 0002-7863
- 1520-5126
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
status: public
title: Aromatic ring dynamics, thermal activation, and transient conformations of
a 468 kDa enzyme by specific 1H–13C labeling and fast magic-angle spinning NMR
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 141
year: '2019'
...
---
_id: '8409'
abstract:
- lang: eng
text: The bacterial cell wall is composed of the peptidoglycan (PG), a large polymer
that maintains the integrity of the bacterial cell. Due to its multi-gigadalton
size, heterogeneity, and dynamics, atomic-resolution studies are inherently complex.
Solid-state NMR is an important technique to gain insight into its structure,
dynamics and interactions. Here, we explore the possibilities to study the PG
with ultra-fast (100 kHz) magic-angle spinning NMR. We demonstrate that highly
resolved spectra can be obtained, and show strategies to obtain site-specific
resonance assignments and distance information. We also explore the use of proton-proton
correlation experiments, thus opening the way for NMR studies of intact cell walls
without the need for isotope labeling.
article_processing_charge: No
article_type: original
author:
- first_name: Catherine
full_name: Bougault, Catherine
last_name: Bougault
- first_name: Isabel
full_name: Ayala, Isabel
last_name: Ayala
- first_name: Waldemar
full_name: Vollmer, Waldemar
last_name: Vollmer
- first_name: Jean-Pierre
full_name: Simorre, Jean-Pierre
last_name: Simorre
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
citation:
ama: Bougault C, Ayala I, Vollmer W, Simorre J-P, Schanda P. Studying intact bacterial
peptidoglycan by proton-detected NMR spectroscopy at 100 kHz MAS frequency. Journal
of Structural Biology. 2019;206(1):66-72. doi:10.1016/j.jsb.2018.07.009
apa: Bougault, C., Ayala, I., Vollmer, W., Simorre, J.-P., & Schanda, P. (2019).
Studying intact bacterial peptidoglycan by proton-detected NMR spectroscopy at
100 kHz MAS frequency. Journal of Structural Biology. Elsevier. https://doi.org/10.1016/j.jsb.2018.07.009
chicago: Bougault, Catherine, Isabel Ayala, Waldemar Vollmer, Jean-Pierre Simorre,
and Paul Schanda. “Studying Intact Bacterial Peptidoglycan by Proton-Detected
NMR Spectroscopy at 100 kHz MAS Frequency.” Journal of Structural Biology.
Elsevier, 2019. https://doi.org/10.1016/j.jsb.2018.07.009.
ieee: C. Bougault, I. Ayala, W. Vollmer, J.-P. Simorre, and P. Schanda, “Studying
intact bacterial peptidoglycan by proton-detected NMR spectroscopy at 100 kHz
MAS frequency,” Journal of Structural Biology, vol. 206, no. 1. Elsevier,
pp. 66–72, 2019.
ista: Bougault C, Ayala I, Vollmer W, Simorre J-P, Schanda P. 2019. Studying intact
bacterial peptidoglycan by proton-detected NMR spectroscopy at 100 kHz MAS frequency.
Journal of Structural Biology. 206(1), 66–72.
mla: Bougault, Catherine, et al. “Studying Intact Bacterial Peptidoglycan by Proton-Detected
NMR Spectroscopy at 100 kHz MAS Frequency.” Journal of Structural Biology,
vol. 206, no. 1, Elsevier, 2019, pp. 66–72, doi:10.1016/j.jsb.2018.07.009.
short: C. Bougault, I. Ayala, W. Vollmer, J.-P. Simorre, P. Schanda, Journal of
Structural Biology 206 (2019) 66–72.
date_created: 2020-09-17T10:29:10Z
date_published: 2019-04-01T00:00:00Z
date_updated: 2021-01-12T08:19:05Z
day: '01'
doi: 10.1016/j.jsb.2018.07.009
extern: '1'
external_id:
pmid:
- '30031884'
intvolume: ' 206'
issue: '1'
keyword:
- Structural Biology
language:
- iso: eng
month: '04'
oa_version: Submitted Version
page: 66-72
pmid: 1
publication: Journal of Structural Biology
publication_identifier:
issn:
- 1047-8477
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: Studying intact bacterial peptidoglycan by proton-detected NMR spectroscopy
at 100 kHz MAS frequency
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 206
year: '2019'
...