The DCCD-reactive aspartyl-residue of subunit C from the Escherichia coli ATP-synthase is important for the conformation of F0.
The effect of various point mutations in subunits a and and c of the E. coli ATP-synthase was characterized. In each of the mutants there was no F0-dependent H+-conduction, but still an ATPase-activity comparable to wildtype activities. In addition, the subunit b could be extracted from the mutant's F0 but not from the F0 of wildtype. The effects are interpreted as a change in the conformation of F0 caused by the different mutations.
D025181:ATP Synthetase Complexes; D001224:Aspartic Acid; D002234:Carbodiimides / Q000494:pharmacology*; D004024:Dicyclohexylcarbodiimide / Q000494:pharmacology*; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D046911:Macromolecular Substances; D009097:Multienzyme Complexes / Q000235:genetics / Q000502:physiology*; D009154:Mutation; D010770:Phosphotransferases / Q000235:genetics / Q000502:physiology*; D011487:Protein Conformation; D006180:Proton-Translocating ATPases / Q000502:physiology*; D013329:Structure-Activity Relationship
D002234:Carbodiimides; D046911:Macromolecular Substances; D009097:Multienzyme Complexes; D001224:Aspartic Acid; D004024:Dicyclohexylcarbodiimide; D010770:Phosphotransferases; D025181:ATP Synthetase Complexes; D006180:Proton-Translocating ATPases