title: Rotational mechanism of Enterococcus hirae V1-ATPase by crystal-structure and single-molecule analyses.
abstract: In ion-transporting rotary ATPases, the mechanical rotation of inner rotor subunits against other stator subunits in the complex mediates conversion of chemical free energy from ATP hydrolysis into electrochemical potential by pumping ions across the cell membrane. To fully understand the rotational mechanism of energy conversion, it is essential to analyze a target sample by multiple advanced methods that differ in spatiotemporal resolutions and sample environments. Here, we describe such a strategy applied to the water-soluble V1 moiety of Enterococcus hirae V-ATPase; this strategy involves integration of crystal structure studies and single-molecule analysis of rotary dynamics and torque generation. In addition, we describe our current model of the chemo-mechanical coupling scheme obtained by this approach, as well as future prospects.
authors: Okazaki Institute for Integrative Bioscience, Institute for Molecular Science, National Institutes of Natural Sciences, Aichi 444-8787, Japan; Department of Functional Molecular Science, School of Physical Sciences, The Graduate University for Advanced Studies (SOKENDAI), Kanagawa 240-0193, Japan. Electronic address: iino@ims.ac.jp.
authors: Ryota
authors: R
authors: Iino
authors: Department of Physics, Faculty of Science and Engineering, Chuo University, Tokyo 112-8551, Japan.
authors: Hiroshi
authors: H
authors: Ueno
authors: Department of Applied Chemistry, The University of Tokyo, Tokyo 113-8656, Japan.
authors: Yoshihiro
authors: Y
authors: Minagawa
authors: Department of Chemistry, Graduate School of Science, Chiba University, Chiba 263-8522, Japan.
authors: Kano
authors: K
authors: Suzuki
authors: Department of Chemistry, Graduate School of Science, Chiba University, Chiba 263-8522, Japan; JST, PRESTO, Chiba 263-8522, Japan. Electronic address: t.murata@faculty.chiba-u.jp.
authors: Takeshi
authors: T
authors: Murata
mesh_terms: D000251:Adenosine Triphosphatases / Q000737:chemistry* / Q000378:metabolism; D001696:Biomechanical Phenomena; D018360:Crystallography, X-Ray / Q000379:methods*; D016983:Enterococcus / Q000201:enzymology*; D006801:Humans; D012399:Rotation; D019415:Torque
chemical_list: D000251:Adenosine Triphosphatases