---
_id: '8581'
abstract:
- lang: eng
  text: The majority of adenosine triphosphate (ATP) powering cellular processes in
    eukaryotes is produced by the mitochondrial F1Fo ATP synthase. Here, we present
    the atomic models of the membrane Fo domain and the entire mammalian (ovine) F1Fo,
    determined by cryo-electron microscopy. Subunits in the membrane domain are arranged
    in the ‘proton translocation cluster’ attached to the c-ring and a more distant
    ‘hook apparatus’ holding subunit e. Unexpectedly, this subunit is anchored to
    a lipid ‘plug’ capping the c-ring. We present a detailed proton translocation
    pathway in mammalian Fo and key inter-monomer contacts in F1Fo multimers. Cryo-EM
    maps of F1Fo exposed to calcium reveal a retracted subunit e and a disassembled
    c-ring, suggesting permeability transition pore opening. We propose a model for
    the permeability transition pore opening, whereby subunit e pulls the lipid plug
    out of the c-ring. Our structure will allow the design of drugs for many emerging
    applications in medicine.
acknowledged_ssus:
- _id: EM-Fac
- _id: ScienComp
acknowledgement: We thank J. Novacek from CEITEC (Brno, Czech Republic) for assistance
  with collecting the FEI Krios dataset and iNEXT for providing access to CEITEC.
  We thank the IST Austria EM facility for access and assistance with collecting the
  FEI Glacios dataset. Data processing was performed at the IST high-performance computing
  cluster. This work has been supported by iNEXT EM HEDC (proposal 4506), funded by
  the Horizon 2020 Programme of the European Commission.
article_processing_charge: No
article_type: original
author:
- first_name: Gergely
  full_name: Pinke, Gergely
  id: 4D5303E6-F248-11E8-B48F-1D18A9856A87
  last_name: Pinke
- first_name: Long
  full_name: Zhou, Long
  id: 3E751364-F248-11E8-B48F-1D18A9856A87
  last_name: Zhou
  orcid: 0000-0002-1864-8951
- first_name: Leonid A
  full_name: Sazanov, Leonid A
  id: 338D39FE-F248-11E8-B48F-1D18A9856A87
  last_name: Sazanov
  orcid: 0000-0002-0977-7989
citation:
  ama: Pinke G, Zhou L, Sazanov LA. Cryo-EM structure of the entire mammalian F-type
    ATP synthase. <i>Nature Structural and Molecular Biology</i>. 2020;27(11):1077-1085.
    doi:<a href="https://doi.org/10.1038/s41594-020-0503-8">10.1038/s41594-020-0503-8</a>
  apa: Pinke, G., Zhou, L., &#38; Sazanov, L. A. (2020). Cryo-EM structure of the
    entire mammalian F-type ATP synthase. <i>Nature Structural and Molecular Biology</i>.
    Springer Nature. <a href="https://doi.org/10.1038/s41594-020-0503-8">https://doi.org/10.1038/s41594-020-0503-8</a>
  chicago: Pinke, Gergely, Long Zhou, and Leonid A Sazanov. “Cryo-EM Structure of
    the Entire Mammalian F-Type ATP Synthase.” <i>Nature Structural and Molecular
    Biology</i>. Springer Nature, 2020. <a href="https://doi.org/10.1038/s41594-020-0503-8">https://doi.org/10.1038/s41594-020-0503-8</a>.
  ieee: G. Pinke, L. Zhou, and L. A. Sazanov, “Cryo-EM structure of the entire mammalian
    F-type ATP synthase,” <i>Nature Structural and Molecular Biology</i>, vol. 27,
    no. 11. Springer Nature, pp. 1077–1085, 2020.
  ista: Pinke G, Zhou L, Sazanov LA. 2020. Cryo-EM structure of the entire mammalian
    F-type ATP synthase. Nature Structural and Molecular Biology. 27(11), 1077–1085.
  mla: Pinke, Gergely, et al. “Cryo-EM Structure of the Entire Mammalian F-Type ATP
    Synthase.” <i>Nature Structural and Molecular Biology</i>, vol. 27, no. 11, Springer
    Nature, 2020, pp. 1077–85, doi:<a href="https://doi.org/10.1038/s41594-020-0503-8">10.1038/s41594-020-0503-8</a>.
  short: G. Pinke, L. Zhou, L.A. Sazanov, Nature Structural and Molecular Biology
    27 (2020) 1077–1085.
date_created: 2020-09-28T08:59:27Z
date_published: 2020-11-01T00:00:00Z
date_updated: 2023-08-22T09:33:09Z
day: '01'
department:
- _id: LeSa
doi: 10.1038/s41594-020-0503-8
external_id:
  isi:
  - '000569299400004'
  pmid:
  - '32929284'
intvolume: '        27'
isi: 1
issue: '11'
language:
- iso: eng
month: '11'
oa_version: None
page: 1077-1085
pmid: 1
publication: Nature Structural and Molecular Biology
publication_identifier:
  eissn:
  - '15459985'
  issn:
  - '15459993'
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
related_material:
  link:
  - description: News on IST Homepage
    relation: press_release
    url: https://ist.ac.at/en/news/structure-of-atpase-solved/
scopus_import: '1'
status: public
title: Cryo-EM structure of the entire mammalian F-type ATP synthase
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 27
year: '2020'
...
---
_id: '6859'
abstract:
- lang: eng
  text: V (vacuolar)/A (archaeal)-type adenosine triphosphatases (ATPases), found
    in archaeaand eubacteria, couple ATP hydrolysis or synthesis to proton translocation
    across theplasma membrane using the rotary-catalysis mechanism. They belong to
    the V-typeATPase family, which differs from the mitochondrial/chloroplast F-type
    ATP synthasesin overall architecture. We solved cryo–electron microscopy structures
    of the intactThermus thermophilusV/A-ATPase, reconstituted into lipid nanodiscs,
    in three rotationalstates and two substates. These structures indicate substantial
    flexibility betweenV1and Voin a working enzyme, which results from mechanical
    competition between centralshaft rotation and resistance from the peripheral stalks.
    We also describedetails of adenosine diphosphate inhibition release, V1-Votorque
    transmission, andproton translocation, which are relevant for the entire V-type
    ATPase family.
acknowledged_ssus:
- _id: ScienComp
article_number: eaaw9144
article_processing_charge: No
author:
- first_name: Long
  full_name: Zhou, Long
  id: 3E751364-F248-11E8-B48F-1D18A9856A87
  last_name: Zhou
  orcid: 0000-0002-1864-8951
- first_name: Leonid A
  full_name: Sazanov, Leonid A
  id: 338D39FE-F248-11E8-B48F-1D18A9856A87
  last_name: Sazanov
  orcid: 0000-0002-0977-7989
citation:
  ama: Zhou L, Sazanov LA. Structure and conformational plasticity of the intact Thermus
    thermophilus V/A-type ATPase. <i>Science</i>. 2019;365(6455). doi:<a href="https://doi.org/10.1126/science.aaw9144">10.1126/science.aaw9144</a>
  apa: Zhou, L., &#38; Sazanov, L. A. (2019). Structure and conformational plasticity
    of the intact Thermus thermophilus V/A-type ATPase. <i>Science</i>. AAAS. <a href="https://doi.org/10.1126/science.aaw9144">https://doi.org/10.1126/science.aaw9144</a>
  chicago: Zhou, Long, and Leonid A Sazanov. “Structure and Conformational Plasticity
    of the Intact Thermus Thermophilus V/A-Type ATPase.” <i>Science</i>. AAAS, 2019.
    <a href="https://doi.org/10.1126/science.aaw9144">https://doi.org/10.1126/science.aaw9144</a>.
  ieee: L. Zhou and L. A. Sazanov, “Structure and conformational plasticity of the
    intact Thermus thermophilus V/A-type ATPase,” <i>Science</i>, vol. 365, no. 6455.
    AAAS, 2019.
  ista: Zhou L, Sazanov LA. 2019. Structure and conformational plasticity of the intact
    Thermus thermophilus V/A-type ATPase. Science. 365(6455), eaaw9144.
  mla: Zhou, Long, and Leonid A. Sazanov. “Structure and Conformational Plasticity
    of the Intact Thermus Thermophilus V/A-Type ATPase.” <i>Science</i>, vol. 365,
    no. 6455, eaaw9144, AAAS, 2019, doi:<a href="https://doi.org/10.1126/science.aaw9144">10.1126/science.aaw9144</a>.
  short: L. Zhou, L.A. Sazanov, Science 365 (2019).
date_created: 2019-09-07T19:04:45Z
date_published: 2019-08-23T00:00:00Z
date_updated: 2023-08-29T07:52:02Z
day: '23'
department:
- _id: LeSa
doi: 10.1126/science.aaw9144
external_id:
  isi:
  - '000482464000043'
  pmid:
  - '31439765'
intvolume: '       365'
isi: 1
issue: '6455'
language:
- iso: eng
month: '08'
oa_version: None
pmid: 1
publication: Science
publication_identifier:
  eissn:
  - 1095-9203
  issn:
  - 0036-8075
publication_status: published
publisher: AAAS
quality_controlled: '1'
related_material:
  link:
  - description: News on IST Website
    relation: press_release
    url: https://ist.ac.at/en/news/structure-of-protein-nano-turbine-revealed/
scopus_import: '1'
status: public
title: Structure and conformational plasticity of the intact Thermus thermophilus
  V/A-type ATPase
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 365
year: '2019'
...
---
_id: '6507'
abstract:
- lang: eng
  text: The osteoclast-associated receptor (OSCAR) is a collagen-binding immune receptor
    with important roles in dendritic cell maturation and activation of inflammatory
    monocytes as well as in osteoclastogenesis. The crystal structure of the OSCAR
    ectodomain is presented, both free and in complex with a consensus triple-helical
    peptide (THP). The structures revealed a collagen-binding site in each immunoglobulin-like
    domain (D1 and D2). The THP binds near a predicted collagen-binding groove in
    D1, but a more extensive interaction with D2 is facilitated by the unusually wide
    D1-D2 interdomain angle in OSCAR. Direct binding assays, combined with site-directed
    mutagenesis, confirm that the primary collagen-binding site in OSCAR resides in
    D2, in marked contrast to the related collagen receptors, glycoprotein VI (GPVI)
    and leukocyte-associated immunoglobulin-like receptor-1 (LAIR-1). Monomeric OSCAR
    D1D2 binds to the consensus THP with a KD of 28 µM measured in solution, but shows
    a higher affinity (KD 1.5 μM) when binding to a solid-phase THP, most likely due
    to an avidity effect. These data suggest a 2-stage model for the interaction of
    OSCAR with a collagen fibril, with transient, low-affinity interactions initiated
    by the membrane-distal D1, followed by firm adhesion to the primary binding site
    in D2.
author:
- first_name: Long
  full_name: Zhou, Long
  id: 3E751364-F248-11E8-B48F-1D18A9856A87
  last_name: Zhou
  orcid: 0000-0002-1864-8951
- first_name: J. M.
  full_name: Hinerman, J. M.
  last_name: Hinerman
- first_name: M.
  full_name: Blaszczyk, M.
  last_name: Blaszczyk
- first_name: J. L. C.
  full_name: Miller, J. L. C.
  last_name: Miller
- first_name: D. G.
  full_name: Conrady, D. G.
  last_name: Conrady
- first_name: A. D.
  full_name: Barrow, A. D.
  last_name: Barrow
- first_name: D. Y.
  full_name: Chirgadze, D. Y.
  last_name: Chirgadze
- first_name: D.
  full_name: Bihan, D.
  last_name: Bihan
- first_name: R. W.
  full_name: Farndale, R. W.
  last_name: Farndale
- first_name: A. B.
  full_name: Herr, A. B.
  last_name: Herr
citation:
  ama: Zhou L, Hinerman JM, Blaszczyk M, et al. Structural basis for collagen recognition
    by the immune receptor OSCAR. <i>Blood</i>. 2015;127(5):529-537. doi:<a href="https://doi.org/10.1182/blood-2015-08-667055">10.1182/blood-2015-08-667055</a>
  apa: Zhou, L., Hinerman, J. M., Blaszczyk, M., Miller, J. L. C., Conrady, D. G.,
    Barrow, A. D., … Herr, A. B. (2015). Structural basis for collagen recognition
    by the immune receptor OSCAR. <i>Blood</i>. American Society of Hematology. <a
    href="https://doi.org/10.1182/blood-2015-08-667055">https://doi.org/10.1182/blood-2015-08-667055</a>
  chicago: Zhou, Long, J. M. Hinerman, M. Blaszczyk, J. L. C. Miller, D. G. Conrady,
    A. D. Barrow, D. Y. Chirgadze, D. Bihan, R. W. Farndale, and A. B. Herr. “Structural
    Basis for Collagen Recognition by the Immune Receptor OSCAR.” <i>Blood</i>. American
    Society of Hematology, 2015. <a href="https://doi.org/10.1182/blood-2015-08-667055">https://doi.org/10.1182/blood-2015-08-667055</a>.
  ieee: L. Zhou <i>et al.</i>, “Structural basis for collagen recognition by the immune
    receptor OSCAR,” <i>Blood</i>, vol. 127, no. 5. American Society of Hematology,
    pp. 529–537, 2015.
  ista: Zhou L, Hinerman JM, Blaszczyk M, Miller JLC, Conrady DG, Barrow AD, Chirgadze
    DY, Bihan D, Farndale RW, Herr AB. 2015. Structural basis for collagen recognition
    by the immune receptor OSCAR. Blood. 127(5), 529–537.
  mla: Zhou, Long, et al. “Structural Basis for Collagen Recognition by the Immune
    Receptor OSCAR.” <i>Blood</i>, vol. 127, no. 5, American Society of Hematology,
    2015, pp. 529–37, doi:<a href="https://doi.org/10.1182/blood-2015-08-667055">10.1182/blood-2015-08-667055</a>.
  short: L. Zhou, J.M. Hinerman, M. Blaszczyk, J.L.C. Miller, D.G. Conrady, A.D. Barrow,
    D.Y. Chirgadze, D. Bihan, R.W. Farndale, A.B. Herr, Blood 127 (2015) 529–537.
date_created: 2019-05-31T09:38:50Z
date_published: 2015-11-02T00:00:00Z
date_updated: 2021-01-12T08:07:47Z
day: '02'
doi: 10.1182/blood-2015-08-667055
extern: '1'
external_id:
  pmid:
  - '26552697'
intvolume: '       127'
issue: '5'
language:
- iso: eng
month: '11'
oa_version: None
page: 529-537
pmid: 1
publication: Blood
publication_identifier:
  issn:
  - 0006-4971
  - 1528-0020
publication_status: published
publisher: American Society of Hematology
quality_controlled: '1'
status: public
title: Structural basis for collagen recognition by the immune receptor OSCAR
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 127
year: '2015'
...