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Cited by 51ATP Synthase and ATPases ResearchAdvanced Electron Microscopy Techniques and ApplicationsEnzyme Structure and Function

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Structure of ATP synthase under strain during catalysis

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Guo, Hui, Rubinstein, John L.·2022·Nature Communications
DOI 10.1038/s41467-022-29893-2PMC PMC9038767

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Abstract

ATP synthases are macromolecular machines consisting of an ATP-hydrolysis-driven F 1 motor and a proton-translocation-driven F O motor. The F 1 and F O motors oppose each other’s action on a shared rotor subcomplex and are held stationary relative to each other by a peripheral stalk. Structures of resting mitochondrial ATP synthases revealed a left-handed curvature of the peripheral stalk even though rotation of the rotor, driven by either ATP hydrolysis in F 1 or proton translocation through F O , would apply a right-handed bending force to the stalk. We used cryoEM to image yeast mitochondrial ATP synthase under strain during ATP-hydrolysis-driven rotary catalysis, revealing a large deformation of the peripheral stalk. The structures show how the peripheral stalk opposes the bending force and suggests that during ATP synthesis proton translocation causes accumulation of strain in the stalk, which relaxes by driving the relative rotation of the rotor through six sub-steps within F 1 , leading to catalysis.

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Metadata

Authors
Guo, H., & Rubinstein, J. L.
Affiliations
University of Toronto (CA)
Corresponding author
Rubinstein, John L.
ORCID
Venue
Nature Communications
Publisher
Springer Science and Business Media LLC
Published
2022-04-25
Volume
13
Issue
1
Pages
2232-2232
ISSN
2041-1723 (ISSN-L)
DOI
10.1038/s41467-022-29893-2
PMC
PMC9038767
OpenAlex
W4225253156
Cited by
51
References
2
Citations by year
2026: 6 · 2025: 14 · 2024: 13 · 2023: 10 · 2022: 8
FWCI
3.67
Type
journal article
Language
en
Update notices
correction (2022-05-17)
Open access
Licence
Locations
  • Nature Communications (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • RePEc: Research Papers in Economics (submittedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
Funders
  • Gouvernement du Canada | Canadian Institutes of Health Research (PJT162186)
  • Canada Research Chairs
  • Canada Foundation for Innovation
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Keywords
ATP synthase, peripheral stalk, mechanical strain, ATP hydrolysis, proton translocation, rotary catalysis, mitochondrial ATP synthase, yeast, cryo-electron microscopy
MeSH terms
Adenosine Triphosphate, Catalysis, Protons, Saccharomyces cerevisiae, Nitric Oxide Synthase, Mitochondrial Proton-Translocating ATPases

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