The molecular structure of an axle-less F₁-ATPase.

ABSTRACT: F₁F_o ATP synthase is a molecular rotary motor that can generate ATP using a transmembrane proton motive force. Isolated F₁-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 F₁-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 F₁ 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 Bacillus sp. PS3 F₁-ATPase. T

SUBMITTER: Furlong EJ 

PROVIDER: S-EPMC11326301 | biostudies-literature | 2024 Aug

REPOSITORIES: biostudies-literature