AUTHOR=Yokoyama Ken 

TITLE=Rotary mechanism of V/A-ATPases—how is ATP hydrolysis converted into a mechanical step rotation in rotary ATPases?

JOURNAL=Frontiers in Molecular Biosciences

VOLUME=10

YEAR=2023

URL=https://www.frontiersin.org/journals/molecular-biosciences/articles/10.3389/fmolb.2023.1176114

DOI=10.3389/fmolb.2023.1176114

ISSN=2296-889X

ABSTRACT=<p>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<sub>1</sub> domain, rotates upon ATP hydrolysis. However, the mechanism by which ATP hydrolysis in the V<sub>1</sub> 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<sub>open</sub>, AB<sub>semi</sub>, and AB<sub>closed</sub>), leading to a 120° rotation of the central rotor. Besides the closing motion caused by ATP bound to AB<sub>open</sub>, the hydrolysis of ATP bound to AB<sub>semi</sub> 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.</p>