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

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.
Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1038/s41467-020-16387-2

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Role:
Author
ORCID:
0000-0001-7220-3120
More by this author
Role:
Author
ORCID:
0000-0001-9964-0929


Publisher:
Springer Nature
Journal:
Nature Communications More from this journal
Volume:
11
Issue:
1
Article number:
2615
Publication date:
2020-05-26
Acceptance date:
2020-04-30
DOI:
EISSN:
2041-1723
Pmid:
32457314

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