Structural snapshots of V/A-ATPase reveal the rotary catalytic mechanism of rotary ATPases.

ABSTRACT: V/A-ATPase is a motor protein that shares a common rotary catalytic mechanism with F_oF₁ ATP synthase. When powered by ATP hydrolysis, the V₁ domain rotates the central rotor against the A₃B₃ hexamer, composed of three catalytic AB dimers adopting different conformations (AB_open, AB_semi, and AB_closed). Here, we report the atomic models of 18 catalytic intermediates of the V₁ domain of V/A-ATPase under different reaction conditions, determined by single particle cryo-EM. The models reveal that the rotor does not rotate immediately after binding of ATP to the V₁. Instead, three events proceed simultaneously with the 120˚ rotation of the shaft: hydrolysis of ATP in AB_semi, zipper movement in AB_open by the binding ATP, and unzipper movement in AB_closed with release of both ADP and Pi. This indicates the unidirectional rotation of V/A-ATPase by a ratchet-like mechanism owing to ATP hydrolysis in AB_semi, rather than the power stroke model proposed previously for F₁-ATPase.

SUBMITTER: Kishikawa J 

PROVIDER: S-EPMC8904598 | biostudies-literature | 2022 Mar

REPOSITORIES: biostudies-literature