@article{0c41144e92884292839fc88a5d43293f,
title = "Rotational mechanism model of the bacterial V1 motor based on structural and computational analyses",
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.",
keywords = "Free energy, Molecular dynamics, Rotary motor, V-ATPase, X-ray structure",
author = "Abhishek Singharoy and Chris Chipot and Toru Ekimoto and Kano Suzuki and Mitsunori Ikeguchi and Ichiro Yamato and Takeshi Murata",
note = "Funding Information: The authors are grateful for funding provided by the National Institute of Health (R01-GM067887-11), by Grant-in-Aid for Scientific Research on Innovative Areas “Molecular Engine” (Grant Nos. 17H03638, 18H05425, and 18H05426) from the Ministry of Education, Culture, Sports, Science and Technology (MEXT), by the Basis for Supporting Innovative Drug Discovery and Life Science Research (BINDS) (Project ID: JP17am0101083, JP17am0101109, and JP18am0101083) from Japan Agency for Medical Research and Development (AMED), by “Priority Issue on Post-K computer” (Building Innovative Drug Discovery Infrastructure Through Functional Control of Biomolecular Systems) (Project ID: hp150269, hp160223, hp170255, and hp180191) from MEXT, and by RIKEN Dynamic Structural Biology Project. This research used resources of the Oak Ridge Leadership Computing Facility at the Oak Ridge National Laboratory, which is supported by the Office of Science of the United States Department of Energy under Contract No. DE-AC05-00OR22725. Publisher Copyright: Copyright {\textcopyright} 2019 Singharoy, Chipot, Ekimoto, Suzuki, Ikeguchi, Yamato and Murata. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.",
year = "2019",
doi = "10.3389/fphys.2019.00046",
language = "English (US)",
volume = "10",
journal = "Frontiers in Physiology",
issn = "1664-042X",
publisher = "Frontiers Research Foundation",
number = "FEB",
}