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• W2599958381 abstract "Enterococcus hirae V1-ATPase is a molecular motor composed of the A3B3 hexamer ring and the central stalk. In association with ATP hydrolysis, three catalytic AB pairs in the A3B3 ring undergo conformational changes, which lead to a 120° rotation of the central stalk. To understand how the conformational changes of three catalytic pairs induce the 120° rotation of the central stalk, we performed multiscale molecular dynamics (MD) simulations in which coarse-grained and all-atom MD simulations were combined using a fluctuation matching methodology. During the rotation, a catalytic AB pair spontaneously adopted an intermediate conformation, which was not included in the initial inputs of the simulations and was essentially close to the “bindable-like” structure observed in a recently solved crystal structure. Furthermore, the creation of a space between the bindable-like and tight pairs was required for the central stalk to rotate without steric hindrance. These cooperative rearrangements of the three catalytic pairs are crucial for the rotation of the central stalk." @default.
• W2599958381 created "2017-04-07" @default.
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• W2599958381 date "2017-03-01" @default.
• W2599958381 modified "2023-10-10" @default.
• W2599958381 title "Rotation Mechanism of Molecular Motor V1-ATPase Studied by Multiscale Molecular Dynamics Simulation" @default.
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• W2599958381 doi "https://doi.org/10.1016/j.bpj.2017.01.029" @default.
• W2599958381 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5355535" @default.
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