The molecular structure of an axle-less F 1 -ATPase

F F ATP synthase is a molecular rotary motor that can generate ATP using a transmembrane proton motive force. Isolated F -ATPase catalytic cores can hydrolyse ATP, passing through a series of conformational states involving rotation of the central γ rotor subunit and the opening and closing of the c...

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Published inbioRxiv
Main Authors Furlong, Emily J, Reininger-Chatzigiannakis, Ian-Blaine P, Zeng, Yi C, Brown, Simon H J, Sobti, Meghna, Stewart, Alastair G
Format Journal Article
LanguageEnglish
Published United States Cold Spring Harbor Laboratory 09.08.2024
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Summary:F F ATP synthase is a molecular rotary motor that can generate ATP using a transmembrane proton motive force. Isolated F -ATPase catalytic cores can hydrolyse ATP, passing through a series of conformational states involving rotation of the central γ rotor subunit and the opening and closing of the catalytic β subunits. Cooperativity in F -ATPase has long thought to be conferred through the γ subunit, with three key interaction sites between the γ and β subunits being identified. Single molecule studies have demonstrated that the F complexes lacking the γ axle still "rotate" and hydrolyse ATP, but with less efficiency. We solved the cryogenic electron microscopy structure of an axle-less sp. PS3 F -ATPase. The unexpected binding-dwell conformation of the structure in combination with the observed lack of interactions between the axle-less γ and the open β subunit suggests that the complete γ subunit is important for coordinating efficient ATP binding of F -ATPase.
ISSN:2692-8205
DOI:10.1101/2024.08.08.607276