Answers are grounded in this paper and cite their sources.
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.
No takes yet. Share an insight, caveat, or question.
Hsu et al. (1987) studied this question.
Synapse has enriched 10 related papers. Consider them for comparative context: