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Cryo-EM structures provide insight into how E. coli F1Fo ATP synthase accommodates symmetry mismatch

Author

Listed:
  • Meghna Sobti

    (The Victor Chang Cardiac Research Institute
    St Vincent’s Clinical School, UNSW Sydney)

  • James L. Walshe

    (The Victor Chang Cardiac Research Institute)

  • Di Wu

    (University of Oxford)

  • Robert Ishmukhametov

    (University of Oxford)

  • Yi C. Zeng

    (The Victor Chang Cardiac Research Institute)

  • Carol V. Robinson

    (University of Oxford)

  • Richard M. Berry

    (University of Oxford)

  • Alastair G. Stewart

    (The Victor Chang Cardiac Research Institute
    St Vincent’s Clinical School, UNSW Sydney)

Abstract

F1Fo ATP synthase functions as a biological rotary generator that makes a major contribution to cellular energy production. It comprises two molecular motors coupled together by a central and a peripheral stalk. Proton flow through the Fo motor generates rotation of the central stalk, inducing conformational changes in the F1 motor that catalyzes ATP production. Here we present nine cryo-EM structures of E. coli ATP synthase to 3.1–3.4 Å resolution, in four discrete rotational sub-states, which provide a comprehensive structural model for this widely studied bacterial molecular machine. We observe torsional flexing of the entire complex and a rotational sub-step of Fo associated with long-range conformational changes that indicates how this flexibility accommodates the mismatch between the 3- and 10-fold symmetries of the F1 and Fo motors. We also identify density likely corresponding to lipid molecules that may contribute to the rotor/stator interaction within the Fo motor.

Suggested Citation

  • Meghna Sobti & James L. Walshe & Di Wu & Robert Ishmukhametov & Yi C. Zeng & Carol V. Robinson & Richard M. Berry & Alastair G. Stewart, 2020. "Cryo-EM structures provide insight into how E. coli F1Fo ATP synthase accommodates symmetry mismatch," Nature Communications, Nature, vol. 11(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-16387-2
    DOI: 10.1038/s41467-020-16387-2
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    Cited by:

    1. Ondřej Gahura & Alexander Mühleip & Carolina Hierro-Yap & Brian Panicucci & Minal Jain & David Hollaus & Martina Slapničková & Alena Zíková & Alexey Amunts, 2022. "An ancestral interaction module promotes oligomerization in divergent mitochondrial ATP synthases," Nature Communications, Nature, vol. 13(1), pages 1-13, December.

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