title: Subunit composition, structure, and distribution of bacterial V-type ATPases.
abstract: The overall structure of V-ATPase complexes resembles that of F-type ATPases, but the stalk region is different and more complex. Database searches followed by sequence analysis of the five water-soluble stalk region subunits C-G revealed that (i) to date V-ATPases are found in 16 bacterial species, (ii) bacterial V-ATPases are closer to archaeal A-ATPases than to eukaryotic V-ATPases, and (iii) different groups of bacterial V-ATPases exist. Inconsistencies in the nomenclature of types and subunits are addressed. Attempts to assign subunit positions in V-ATPases based on biochemical experiments, chemical cross-linking, and electron microscopy are discussed. A structural model for prokaryotic and eukaryotic V-ATPases is proposed. The prokaryotic V-ATPase is considered to have a central stalk between headpiece and membrane flanked by two peripheral stalks. The eukaryotic V-ATPases have one additional peripheral stalk.
authors.affiliation: Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Groningen, The Netherlands. j.s.lolkema@biol.rug.nl
authors.forename: Juke S
authors.initials: JS
authors.lastname: Lolkema
authors.forename: Yuriy
authors.initials: Y
authors.lastname: Chaban
authors.forename: Egbert J
authors.initials: EJ
authors.lastname: Boekema
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D017124:Conserved Sequence; D019143:Evolution, Molecular; D008958:Models, Molecular; D020836:Protein Structure, Quaternary; D021122:Protein Subunits / Q000235:genetics; D025262:Vacuolar Proton-Translocating ATPases / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D021122:Protein Subunits; D025262:Vacuolar Proton-Translocating ATPases