Changes Within the Central Stalk of E. Coli FF ATP Synthase Observed After Addition of ATP

Overview

Journal Commun Biol

Specialty Biology

Date 2023 Jan 11

PMID 36631659

Authors

Meghna Sobti

Yi C Zeng

James L Walshe

Simon H J Brown

Robert Ishmukhametov

Alastair G Stewart

Affiliations

Soon will be listed here.

Abstract

FF ATP synthase functions as a biological generator and makes a major contribution to cellular energy production. Proton flow generates rotation in the F motor that is transferred to the F motor to catalyze ATP production, with flexible F/F coupling required for efficient catalysis. FF 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 FF 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 F motor. This highlights the importance of the central rotor for flexible coupling of the F and F motors and provides further insight into the regulatory mechanism mediated by subunit ε.

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