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Subunit epsilon of E. coli F1Fo ATP synthase attenuates enzyme activity by modulating central stalk flexibility

View ORCID ProfileMeghna Sobti, View ORCID ProfileJames L. Walshe, Yi C. Zeng, Robert Ishmukhametov, View ORCID ProfileAlastair G. Stewart
doi: https://doi.org/10.1101/2020.09.30.320408
Meghna Sobti
1Molecular, Structural and Computational Biology Division, The Victor Chang Cardiac Research Institute, Darlinghurst, Australia
2St Vincent’s Clinical School, Faculty of Medicine, UNSW Sydney, Kensington, Australia
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James L. Walshe
1Molecular, Structural and Computational Biology Division, The Victor Chang Cardiac Research Institute, Darlinghurst, Australia
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Yi C. Zeng
1Molecular, Structural and Computational Biology Division, The Victor Chang Cardiac Research Institute, Darlinghurst, Australia
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Robert Ishmukhametov
3Department of Physics, Clarendon Laboratory, University of Oxford, Oxford, United Kingdom
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Alastair G. Stewart
1Molecular, Structural and Computational Biology Division, The Victor Chang Cardiac Research Institute, Darlinghurst, Australia
2St Vincent’s Clinical School, Faculty of Medicine, UNSW Sydney, Kensington, Australia
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  • For correspondence: a.stewart@victorchang.edu.au
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ABSTRACT

F1Fo ATP synthase functions as a biological rotary generator that makes a major contribution to cellular energy production. Proton flow through the Fo motor generates rotation of the central stalk, inducing conformational changes in the F1 motor that catalyzes ATP production via flexible coupling. Here we present a range of cryo-EM structures of E. coli ATP synthase in different rotational and inhibited states observed following a 45 second incubation with 10 mM MgATP. The structures generated describe multiple changes that occur following addition of MgATP, with the inhibitory C-terminal domain of subunit ε (εCTD) disassociating from the central stalk to adopt a condensed “down” conformation. The transition to the εCTD down state increases the torsional flexibility of the central stalk allowing its foot to rotate by ∼50°, with further flexing in the peripheral stalk enabling the c-ring to rotate by two sub-steps in the Fo motor. Truncation mutants lacking the second helix of the εCTD suggest that central stalk rotational flexibility is important for F1Fo ATP synthase function. Overall this study identifies the potential role played by torsional flexing within the rotor and how this could be influenced by the ε subunit.

Competing Interest Statement

The authors have declared no competing interest.

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The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-NC-ND 4.0 International license.
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Posted September 30, 2020.
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Subunit epsilon of E. coli F1Fo ATP synthase attenuates enzyme activity by modulating central stalk flexibility
Meghna Sobti, James L. Walshe, Yi C. Zeng, Robert Ishmukhametov, Alastair G. Stewart
bioRxiv 2020.09.30.320408; doi: https://doi.org/10.1101/2020.09.30.320408
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Subunit epsilon of E. coli F1Fo ATP synthase attenuates enzyme activity by modulating central stalk flexibility
Meghna Sobti, James L. Walshe, Yi C. Zeng, Robert Ishmukhametov, Alastair G. Stewart
bioRxiv 2020.09.30.320408; doi: https://doi.org/10.1101/2020.09.30.320408

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