title: Structure of the vacuolar adenosine triphosphatases.
abstract: Vacuolar adenosine triphosphatases (V-ATPases) represent an important class of proton pumps found in endomembrane systems of eucaryotic cells, where they are involved in pH regulation. Progress has been made in the structure determination of this large, membrane-bound multisubunit enzyme complex. Electron microscopy of the V-ATPase has revealed a ball-and-stalk-like structure similar to F1F0-type ATP synthase, to which the V-ATPase is evolutionary related. Aside from the overall structural similarity of the V-ATPase and F-ATP synthase, a number of distinct structural differences exist between the two related enzymes, giving clues to their different function and regulation in the organism.
authors.affiliation: University of California, Riverside, Department of Biochemistry, 92521, USA. stephan.wilkens@ucr.edu
authors.forename: S
authors.initials: S
authors.lastname: Wilkens
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D001921:Brain / Q000648:ultrastructure; D002417:Cattle; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D008854:Microscopy, Electron; D008954:Models, Biological; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000502:physiology; D011522:Protons
chemical_list: D011522:Protons; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases