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 V domain, rotates upon ATP hydrolysis. However, the mechanism by which ATP hydrolysis in the V 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, AB, and AB), leading to a 120° rotation of the central rotor. Besides the closing motion caused by ATP bound to AB, the hydrolysis of ATP bound to AB drives the 120° step. Our recent time-resolved cryo-EM snapshot analysis provides further evidence for this model. This review aimed to provide a comprehensive overview of the structure and function of V/A-ATPase from a thermophilic bacterium, one of the most well-studied rotary ATPases to date.
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| http://dx.doi.org/10.3389/fmolb.2023.1176114 | DOI Listing |
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