---
_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'
...