title: Molecular structure and rotary dynamics of Enterococcus hirae V₁-ATPase.
abstract: V1-ATPase is a rotary molecular motor in which the mechanical rotation of the rotor DF subunits against the stator A3B3 ring is driven by the chemical free energy of ATP hydrolysis. Recently, using X-ray crystallography, we solved the high-resolution molecular structure of Enterococcus hirae V1-ATPase (EhV1) and revealed how the three catalytic sites in the stator A3B3 ring change their structure on nucleotide binding and interaction with the rotor DF subunits. Furthermore, recently, we also demonstrated directly the rotary catalysis of EhV1 by using single-molecule high-speed imaging and analyzed the properties of the rotary motion in detail. In this critical review, we introduce the molecular structure and rotary dynamics of EhV1 and discuss a possible model of its chemomechanical coupling scheme.
authors.affiliation: Department of Bioorganization Research, Okazaki Institute for Integrative Bioscience, Institute for Molecular Science, National Institutes of Natural Sciences, Aichi, Japan; Department of Functional Molecular Science, School of Physical Sciences, Graduate University for Advanced Studies (SOKENDAI), Kanagawa, Japan.
authors.forename: Ryota
authors.initials: R
authors.lastname: Iino
authors.forename: Yoshihiro
authors.initials: Y
authors.lastname: Minagawa
authors.forename: Hiroshi
authors.initials: H
authors.lastname: Ueno
authors.forename: Mayu
authors.initials: M
authors.lastname: Hara
authors.forename: Takeshi
authors.initials: T
authors.lastname: Murata
mesh_terms: D020134:Catalytic Domain / Q000235:genetics; D018360:Crystallography, X-Ray; D016983:Enterococcus / Q000201:enzymology*; D008958:Models, Molecular; D057054:Molecular Imaging / Q000379:methods; D011487:Protein Conformation; D012399:Rotation; D025262:Vacuolar Proton-Translocating ATPases / Q000737:chemistry*
chemical_list: D025262:Vacuolar Proton-Translocating ATPases
keywords: enzyme mechanisms; protein structure; structural biology