Rotational Mechanism Model of the Bacterial V1 Motor Based on Structural and Computational Analyses
- Arizona State Univ., Tempe, AZ (United States)
- Université de Lorraine, Nancy (France); Univ. of Illinois at Urbana-Champaign, IL (United States)
- Yokohama City University (Japan)
- Chiba University (Japan)
- Yokohama City University (Japan); RIKEN Medical Sciences Innovation Hub Program, Yokohama (Japan)
- Chiba University (Japan); Tokyo University of Science (Japan)
- Chiba University (Japan); Japan Science and Technology Agency (JST), Chiba (Japan)
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. Finally 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.
- Research Organization:
- Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). Oak Ridge Leadership Computing Facility (OLCF)
- Sponsoring Organization:
- USDOE Office of Science (SC); National Institutes of Health (NIH); Ministry of Education, Culture, Sports, Science and Technology (MEXT); Japan Agency for Medical Research and Development (AMED)
- Grant/Contract Number:
- AC05-00OR22725; 17H03638; 18H05425; 18H05426
- OSTI ID:
- 1565788
- Journal Information:
- Frontiers in Physiology, Vol. 10; ISSN 1664-042X
- Publisher:
- Frontiers Media S.A.Copyright Statement
- Country of Publication:
- United States
- Language:
- English
Web of Science
Structure and conformational plasticity of the intact Thermus thermophilus V/A-type ATPase
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journal | August 2019 |
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