biostudies-literatureUnknown10Yokoyama KV/A-ATPase is a rotary molecular motor protein that produces ATP through the rotation of its central rotor. The soluble part of this protein, the V₁ domain, rotates upon ATP hydrolysis. However, the mechanism by which ATP hydrolysis in the V₁ domain couples with the mechanical rotation of the rotor is still unclear. Cryo-EM snapshot analysis of V/A-ATPase indicated that three independent and simultaneous catalytic events occurred at the three catalytic dimers (AB_open, AB_semi, and AB_closed), leading to a 120° rotation of the central rotor. Besides the closing motion caused by ATP bound to AB_open, the hydrolysis of ATP bound to AB_semi drives the 120° step. Our recent time-resolved cryo-EM snapshot analysis provides Frontiers in molecular biosciences1176114https://www.ebi.ac.uk/biostudies/studies/S-EPMC10166205biostudies-literatureRotary mechanism of V/A-ATPases-how is ATP hydrolysis converted into a mechanical step rotation in rotary ATPases?PMC10166205Yokoyama KfalseRotary mechanism of V/A-ATPases-how is ATP hydrolysis converted into a mechanical step rotation in rotary ATPases?V/A-ATPase is a rotary molecular motor protein that produces ATP through the rotation of its central rotor. The soluble part of this protein, the V₁ domain, rotates upon ATP hydrolysis. However, the mechanism by which ATP hydrolysis in the V₁ domain couples with the mechanical rotation of the rotor is still unclear. Cryo-EM snapshot analysis of V/A-ATPase indicated that three independent and simultaneous catalytic events occurred at the three catalytic dimers (AB_open, AB_semi, and AB_closed), leading to a 120° rotation of the central rotor. Besides the closing motion caused by ATP bound to AB_open, the hydrolysis of ATP bound to AB_semi drives the 120° step. Our recent time-resolved cryo-EM snapshot analysis provides 2023-01-01T00:00:00Z20232025-04-22T02:24:38.884Z2025-02-18T23:43:55.488ZS-EPMC101662053716825710.3389/fmolb.2023.1176114