Rotation Mechanism of Molecular Motor V₁-ATPase Studied by Multiscale Molecular Dynamics Simulation.

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 "

SUBMITTER: Isaka Y 

PROVIDER: S-EPMC5355535 | biostudies-literature | 2017 Mar

REPOSITORIES: biostudies-literature