title: Crystal structure of the central axis DF complex of the prokaryotic V-ATPase.
abstract: V-ATPases function as ATP-dependent ion pumps in various membrane systems of living organisms. ATP hydrolysis causes rotation of the central rotor complex, which is composed of the central axis D subunit and a membrane c ring that are connected by F and d subunits. Here we determined the crystal structure of the DF complex of the prokaryotic V-ATPase of Enterococcus hirae at 2.0-Å resolution. The structure of the D subunit comprised a long left-handed coiled coil with a unique short β-hairpin region that is effective in stimulating the ATPase activity of V(1)-ATPase by twofold. The F subunit is bound to the middle portion of the D subunit. The C-terminal helix of the F subunit, which was believed to function as a regulatory region by extending into the catalytic A(3)B(3) complex, contributes to tight binding to the D subunit by forming a three-helix bundle. Both D and F subunits are necessary to bind the d subunit that links to the c ring. From these findings, we modeled the entire rotor complex (DFdc ring) of V-ATPase.
authors: Department of Biological Science and Technology, Tokyo University of Science, 2641 Yamazaki, Noda-shi, Chiba 278-8510, Japan.
authors: Shinya
authors: S
authors: Saijo
authors: Satoshi
authors: S
authors: Arai
authors: K M Mozaffor
authors: KM
authors: Hossain
authors: Ichiro
authors: I
authors: Yamato
authors: Kano
authors: K
authors: Suzuki
authors: Yoshimi
authors: Y
authors: Kakinuma
authors: Yoshiko
authors: Y
authors: Ishizuka-Katsura
authors: Noboru
authors: N
authors: Ohsawa
authors: Takaho
authors: T
authors: Terada
authors: Mikako
authors: M
authors: Shirouzu
authors: Shigeyuki
authors: S
authors: Yokoyama
authors: So
authors: S
authors: Iwata
authors: Takeshi
authors: T
authors: Murata
mesh_terms: D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D016983:Enterococcus / Q000201:enzymology*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011387:Prokaryotic Cells / Q000201:enzymology*; D017433:Protein Structure, Secondary; D021122:Protein Subunits / Q000737:chemistry* / Q000378:metabolism; D016415:Sequence Alignment; D055672:Static Electricity; D040681:Structural Homology, Protein; D025262:Vacuolar Proton-Translocating ATPases / Q000737:chemistry* / Q000378:metabolism
chemical_list: D021122:Protein Subunits; D025262:Vacuolar Proton-Translocating ATPases