Journal article
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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(Preview, Version of record, 2.7MB, Terms of use)
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- Publisher copy:
- 10.1038/s41467-020-16387-2
Authors
- 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:
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2041-1723
- Pmid:
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32457314
- Language:
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English
- Keywords:
- Pubs id:
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1107418
- Local pid:
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pubs:1107418
- Deposit date:
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2021-04-28
Terms of use
- Copyright holder:
- M Sobti et al.
- Copyright date:
- 2020
- Rights statement:
- © The Author(s) 2020. Open Access: This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/ licenses/by/4.0/.
- Licence:
- CC Attribution (CC BY)
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