Topological and functional aspects of the proton conductor, F0, of the Escherichia coli ATP-synthase.
The isolated H+ conductor, F0, of the Escherichia coli ATP-synthase consists of three subunits, a, b, and c. H+-permeable liposomes can be reconstituted with F0 and lipids; addition of F1-ATPase reconstitutes a functional ATP-synthase. Mutants with altered or missing F0 subunits are defective in H+ conduction. Thus, all three subunits are necessary for the expression of H+ conduction. The subunits a and b contain binding sites for F1. Computer calculations, cross-links, membrane-permeating photo-reactive labels, and proteases were used to develop tentative structural models for the individual F0 subunits.
D025181:ATP Synthetase Complexes; D000251:Adenosine Triphosphatases / Q000235:genetics / Q000378:metabolism*; D002462:Cell Membrane / Q000201:enzymology; D004926:Escherichia coli / Q000201:enzymology*; D005796:Genes; D008081:Liposomes; D046911:Macromolecular Substances; D008565:Membrane Proteins / Q000378:metabolism*; D009097:Multienzyme Complexes / Q000378:metabolism*; D009154:Mutation; D009876:Operon; D010770:Phosphotransferases / Q000378:metabolism*; D006180:Proton-Translocating ATPases
D008081:Liposomes; D046911:Macromolecular Substances; D008565:Membrane Proteins; D009097:Multienzyme Complexes; D010770:Phosphotransferases; D025181:ATP Synthetase Complexes; D000251:Adenosine Triphosphatases; D006180:Proton-Translocating ATPases