1H8E

(ADP.AlF4)2(ADP.SO4) bovine F1-ATPase (all three catalytic sites occupied)

1H8E の概要

• エントリーDOI: 10.2210/pdb1h8e/pdb
• 関連するPDBエントリー: 1BMF 1COW 1E1Q 1E1R 1E79 1EFR 1H8H 1NBM 1QO1
• 分子名称: BOVINE MITOCHONDRIAL F1-ATPASE, SULFATE ION, ADENOSINE-5'-DIPHOSPHATE, ... (11 entities in total)
• 機能のキーワード: hydrolase, atp phosphorylase, atp phosphorylase (h+ transporting), atp synthase, f1fo atp synthase, f1-atpase
• 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: 375479.73

構造登録者

Menz, R.I.,Walker, J.E.,Leslie, A.G.W. (登録日: 2001-02-02, 公開日: 2001-08-10, 最終更新日: 2023-12-13)

主引用文献

Menz, R.I.,Walker, J.E.,Leslie, A.G.W.
Structure of Bovine Mitochondrial F1-ATPase with Nucleotide Bound to All Three Catalytic Sites: Implications for the Mechanism of Rotary Catalysis
Cell(Cambridge,Mass.), 106:331-, 2001

PubMed Abstract: The crystal structure of a novel aluminium fluoride inhibited form of bovine mitochondrial F(1)-ATPase has been determined at 2 A resolution. In contrast to all previously determined structures of the bovine enzyme, all three catalytic sites are occupied by nucleotide. The subunit that did not bind nucleotide in previous structures binds ADP and sulfate (mimicking phosphate), and adopts a "half-closed" conformation. This structure probably represents the posthydrolysis, pre-product release step on the catalytic pathway. A catalytic scheme for hydrolysis (and synthesis) at physiological rates and a mechanism for the ATP-driven rotation of the gamma subunit are proposed based on the crystal structures of the bovine enzyme.

PubMed: 11509182
DOI: 10.1016/S0092-8674(01)00452-4

実験手法

X-RAY DIFFRACTION (2 Å)