title: Beta-subunit of Escherichia coli F1-ATPase. An amino acid replacement within a conserved sequence (G-X-X-X-X-G-K-T/S) of nucleotide-binding proteins.
abstract: A mutant strain KF87 of E. coli with a defective beta-subunit (Ala-151----Val) of F1-ATPase was isolated. The mutation is within the conserved sequence (G-X-X-X-X-G-K-T/S) of nucleotide-binding proteins. The mutant F1-ATPase had a much higher rate of uni-site hydrolysis of ATP than the wild type, and about 6% of the wild-type multi-site activity. The mutant enzyme showed defective transmission of conformational change(s) between the ligand- and aurovertin-binding sites.
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D000595:Amino Acid Sequence; D001313:Aurovertins / Q000378:metabolism; D001483:Base Sequence; D002352:Carrier Proteins / Q000235:genetics*; D002373:Cyclic AMP Receptor Protein; D004274:DNA, Recombinant; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D006868:Hydrolysis; D009154:Mutation; D009857:Oncogenes; D010710:Phosphates / Q000378:metabolism; D006180:Proton-Translocating ATPases / Q000235:genetics*
chemical_list: D001313:Aurovertins; D002352:Carrier Proteins; D002373:Cyclic AMP Receptor Protein; D004274:DNA, Recombinant; D010710:Phosphates; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases