Hsu S Y, Noumi T, Takeyama M, Maeda M, Ishibashi S, Futai M
FEBS Lett. 1987 Jun 29;218(2):222-6. doi: 10.1016/0014-5793(87)81050-5.
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.
分离出了一种大肠杆菌突变株KF87,其F1 - ATP酶的β亚基(丙氨酸-151→缬氨酸)存在缺陷。该突变位于核苷酸结合蛋白的保守序列(G - X - X - X - X - G - K - T/S)内。突变型F1 - ATP酶的ATP单位点水解速率比野生型高得多,约为野生型多位点活性的6%。突变酶在配体结合位点和金雀花碱结合位点之间的构象变化传递存在缺陷。