title: Structure of the C subunit of V-type ATPase from Thermus thermophilus at 1.85 A resolution.
abstract: The V-type H(+)-ATPases are similar to the F-type ATP synthases in their structure and functional mechanism. They hydrolyze ATP coupled with proton translocation across a membrane, but in some archaea and eubacteria they also synthesize ATP in the reverse reaction. The C subunit is one of the components of the membrane-bound V(0) moiety of V-type ATPases. The C subunit of V-type H(+)-ATPase from Thermus thermophilus was crystallized in a monoclinic form and its crystal structure was determined at 1.85 A resolution by the MAD method using selenomethionyl protein. The structure has a cone (tapered cylinder) shape consisting of only two types of helix (long and short) as secondary-structure elements. The molecule is divided into three similar domains, each of which has essentially the same topology. On the basis of the structural features and molecular-surface charge distribution, it is suggested that the bottom side of the C subunit is a possible binding site for the V(0) proteolipid L-subunit ring and that the C subunit might function as a spacer unit between the proteolipid L-subunit ring and the rotating V(1) central shaft.
authors.affiliation: Department of Chemistry, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.
authors.forename: Nobutaka
authors.initials: N
authors.lastname: Numoto
authors.forename: Akiko
authors.initials: A
authors.lastname: Kita
authors.forename: Kunio
authors.initials: K
authors.lastname: Miki
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D021122:Protein Subunits; D011510:Proteolipids / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry; D017386:Sequence Homology, Amino Acid; D016963:Thermus thermophilus / Q000201:enzymology*; D025262:Vacuolar Proton-Translocating ATPases / Q000737:chemistry* / Q000378:metabolism
chemical_list: D021122:Protein Subunits; D011510:Proteolipids; D029701:Saccharomyces cerevisiae Proteins; C447616:VMA5 protein, S cerevisiae; D025262:Vacuolar Proton-Translocating ATPases