Sobti, Meghna and Walshe, James L. and Wu, Di and Ishmukhametov, Robert and Zeng, Yi C. and Robinson, Carol V. and Berry, Richard M. and Stewart, Alastair G. (2020) Cryo-EM structures provide insight into how E. coli F1Fo ATP synthase accommodates symmetry mismatch. Nature Communications, 11 (1). p. 2615. ISSN 2041-1723
Preview |
Text
CryoEM-structures-provide-insight-into-how-E-coli-F1Fo-ATP-synthase-accommodates-symmetry-mismatchNature-Communications.pdf Available under License Creative Commons Attribution No Derivatives. Download (2MB) | Preview |
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.
| Item Type: | Article |
|---|---|
| Subjects: | R Medicine > R Medicine (General) |
| Depositing User: | Repository Administrator |
| Date Deposited: | 02 Jun 2020 03:49 |
| Last Modified: | 19 Oct 2021 03:56 |
| URI: | https://eprints.victorchang.edu.au/id/eprint/980 |
Actions (login required)
 |
View Item |