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

Meghna Sobti, James L. Walshe, Di Wu, Robert Ishmukhametov, Yi C. Zeng, Carol V. Robinson, Richard M. Berry and Alastair G. Stewart ()
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Meghna Sobti: The Victor Chang Cardiac Research Institute
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

Nature Communications, 2020, vol. 11, issue 1, 1-10

Abstract: 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.

Date: 2020
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DOI: 10.1038/s41467-020-16387-2

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