title: F-type or V-type? The chimeric nature of the archaebacterial ATP synthase.
abstract: Archaebacterial plasma membranes contain an ATPase acting in vivo as a delta mu H(+)-driven ATP synthase. While functional features and their general structural design are resembling F-type ATPases, primary sequences of the two large polypeptides from the catalytic part are closely related to V-type ATPases from eucaryotic vacuolar membranes. The chimeric nature of archaebacterial ATPase from Sulfolobus was investigated in terms of nucleotide interactions and related to specific sequence parameters in a comparison to well known F- and V-type ATPases. The study disclosed a general difference of F- and V-type ATPases at one class of the nucleotide binding sites.
authors.affiliation: Institute of Biochemistry, Medical University of Lübeck, Germany.
authors.forename: G
authors.initials: G
authors.lastname: Schäfer
authors.forename: M
authors.initials: M
authors.lastname: Meyering-Vos
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001105:Archaea / Q000201:enzymology*; D001665:Binding Sites; D002678:Chimera; D008969:Molecular Sequence Data; D011487:Protein Conformation; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000378:metabolism; D016415:Sequence Alignment
chemical_list: D006180:Proton-Translocating ATPases