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- W2912946070 abstract "V1-ATPase exemplifies the ubiquitous rotary motor, in which a central shaft DF complex rotates inside a hexagonally arranged catalytic A3B3 complex, powered by the energy from ATP hydrolysis. We have recently reported a number of crystal structures of the Enterococcus hirae A3B3DF (V1) complex corresponding to its nucleotide-bound intermediate states, namely the forms waiting for ATP hydrolysis (denoted as catalytic dwell), ATP binding (ATP-binding dwell), and ADP release (ADP-release dwell) along the rotatory catalytic cycle of ATPase. Furthermore, we have performed microsecond-scale molecular dynamics simulations and free-energy calculations to investigate the conformational transitions between these intermediate states and to probe the long-time dynamics of the molecular motor. In this article, the molecular structure and dynamics of the V1-ATPase are reviewed to bring forth a unified model of the motor’s remarkable rotational mechanism." @default.
- W2912946070 created "2019-02-21" @default.
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- W2912946070 date "2019-02-05" @default.
- W2912946070 modified "2023-10-07" @default.
- W2912946070 title "Rotational Mechanism Model of the Bacterial V1 Motor Based on Structural and Computational Analyses" @default.
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- W2912946070 doi "https://doi.org/10.3389/fphys.2019.00046" @default.
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