Mechanism of ATP hydrolysis dependent rotation of bacterial ATP synthase.

ABSTRACT: F₁ domain of ATP synthase is a rotary ATPase complex in which rotation of central γ-subunit proceeds in 120° steps against a surrounding α₃β₃ fueled by ATP hydrolysis. How the ATP hydrolysis reactions occurring in three catalytic αβ dimers are coupled to mechanical rotation is a key outstanding question. Here we describe catalytic intermediates of the F₁ domain in F_oF₁ synthase from Bacillus PS3 sp. during ATP mediated rotation captured using cryo-EM. The structures reveal that three catalytic events and the first 80° rotation occur simultaneously in F₁ domain when nucleotides are bound at all the three catalytic αβ dimers. The remaining 40° rotation of the complete 120° step is driven by completion of ATP hydroly

SUBMITTER: Nakano A 

PROVIDER: S-EPMC10333338 | biostudies-literature | 2023 Jul

REPOSITORIES: biostudies-literature