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

ABSTRACT

F 1 F o ATP synthase is a molecular rotary motor that can generate ATP using a transmembrane proton motive force. Isolated F 1 -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 ß subunits. Cooperativity in F 1 -ATPase has long thought to be conferred through the γ subunit, with three key interaction sites between the γ and ß subunits being identified. Single molecule studies have demonstrated that the F 1 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 F 1 -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 ß subunit suggests that the complete γ subunit is important for coordinating efficient ATP binding of F 1 -ATPase.