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Changes within the central stalk of E. coli F1Fo ATP synthase observed after addition of ATP

Abstract:

F1Fo ATP synthase functions as a biological generator and makes a major contribution to cellular energy production. Proton flow generates rotation in the Fo motor that is transferred to the F1 motor to catalyze ATP production, with flexible F1/Fo coupling required for efficient catalysis. F1Fo ATP synthase can also operate in reverse, hydrolyzing ATP and pumping protons, and in bacteria this function can be regulated by an inhibitory ε subunit. Here we present cryo-EM data showing E. coli F1Fo ATP synthase in different rotational and inhibited sub-states, observed following incubation with 10 mM MgATP. Our structures demonstrate how structural transitions within the inhibitory ε subunit induce torsional movement in the central stalk, thereby enabling its rotation within the Fο motor. This highlights the importance of the central rotor for flexible coupling of the F1 and Fo motors and provides further insight into the regulatory mechanism mediated by subunit ε.

Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1038/s42003-023-04414-z

Authors


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Role:
Author
ORCID:
0000-0001-9964-0929
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Institution:
University of Oxford
Division:
MPLS
Department:
Physics
Role:
Author


Publisher:
Springer Nature
Journal:
Communications Biology More from this journal
Volume:
6
Article number:
26
Publication date:
2023-01-11
Acceptance date:
2023-01-03
DOI:
EISSN:
2399-3642
Pmid:
36631659


Language:
English
Keywords:
Pubs id:
1326838
Local pid:
pubs:1326838
Deposit date:
2023-07-28

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