Rotational mechanism model of the bacterial V1 motor based on structural and computational analyses

Abhishek Singharoy, Chris Chipot, Toru Ekimoto, Kano Suzuki, Mitsunori Ikeguchi, Ichiro Yamato, Takeshi Murata

Research output: Contribution to journalReview articlepeer-review

5 Scopus citations


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.

Original languageEnglish (US)
Article number46
JournalFrontiers in Physiology
Issue numberFEB
StatePublished - 2019


  • Free energy
  • Molecular dynamics
  • Rotary motor
  • V-ATPase
  • X-ray structure

ASJC Scopus subject areas

  • Physiology
  • Physiology (medical)


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