2CK3
Azide inhibited bovine F1-ATPase
2CK3 の概要
| エントリーDOI | 10.2210/pdb2ck3/pdb |
| 関連するPDBエントリー | 1BMF 1COW 1E1Q 1E1R 1E79 1EFR 1H8E 1H8H 1NBM 1OHH 1QO1 1W0J 1W0K |
| 分子名称 | ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL, PHOSPHATE ION, ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL, ... (11 entities in total) |
| 機能のキーワード | hydrolase |
| 由来する生物種 | BOS TAURUS (BOVINE) 詳細 |
| 細胞内の位置 | Mitochondrion inner membrane (By similarity): P19483 Mitochondrion: P00829 P05631 P05630 P05632 |
| タンパク質・核酸の鎖数 | 9 |
| 化学式量合計 | 374810.81 |
| 構造登録者 | Bowler, M.W.,Montgomery, M.G.,Leslie, A.G.W.,Walker, J.E. (登録日: 2006-04-10, 公開日: 2006-05-08, 最終更新日: 2023-12-13) |
| 主引用文献 | Bowler, M.W.,Montgomery, M.G.,Leslie, A.G.,Walker, J.E. How Azide Inhibits ATP Hydrolysis by the F-Atpases. Proc.Natl.Acad.Sci.USA, 103:8646-, 2006 Cited by PubMed Abstract: In the structure of bovine F1-ATPase determined at 1.95-A resolution with crystals grown in the presence of ADP, 5'-adenylyl-imidodiphosphate, and azide, the azide anion interacts with the beta-phosphate of ADP and with residues in the ADP-binding catalytic subunit, betaDP. It occupies a position between the catalytically essential amino acids, beta-Lys-162 in the P loop and the "arginine finger" residue, alpha-Arg-373, similar to the site occupied by the gamma-phosphate in the ATP-binding subunit, betaTP. Its presence in the betaDP-subunit tightens the binding of the side chains to the nucleotide, enhancing its affinity and thereby stabilizing the state with bound ADP. This mechanism of inhibition appears to be common to many other ATPases, including ABC transporters, SecA, and DNA topoisomerase IIalpha. It also explains the stimulatory effect of azide on ATP-sensitive potassium channels by enhancing the binding of ADP. PubMed: 16728506DOI: 10.1073/PNAS.0602915103 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.95 Å) |
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