1OHH

BOVINE MITOCHONDRIAL F1-ATPASE complexed with the inhibitor protein IF1

1OHH の概要

• エントリーDOI: 10.2210/pdb1ohh/pdb
• 関連するPDBエントリー: 1BMF 1COW 1E1Q 1E1R 1E79 1EFR 1GMJ 1H8E 1H8H 1HF9 1NBM 1QO1
• 分子名称: ATP synthase subunit alpha, mitochondrial, ATP synthase subunit beta, mitochondrial, ATP synthase subunit gamma, mitochondrial, ... (6 entities in total)
• 機能のキーワード: synthase, 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 P01096
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 363619.85

構造登録者

Cabezon, E.,Montgomery, M.G.,Leslie, A.G.W.,Walker, J.E. (登録日: 2003-05-27, 公開日: 2003-06-09, 最終更新日: 2023-12-13)

主引用文献

Cabezon, E.,Montgomery, M.G.,Leslie, A.G.W.,Walker, J.E.
The Structure of Bovine F1-ATPase in Complex with its Regulatory Protein If1
Nat.Struct.Biol., 10:744-, 2003

PubMed Abstract: In mitochondria, the hydrolytic activity of ATP synthase is prevented by an inhibitor protein, IF1. The active bovine protein (84 amino acids) is an alpha-helical dimer with monomers associated via an antiparallel alpha-helical coiled coil composed of residues 49-81. The N-terminal inhibitory sequences in the active dimer bind to two F1-ATPases in the presence of ATP. In the crystal structure of the F1-IF1 complex at 2.8 A resolution, residues 1-37 of IF1 bind in the alpha(DP)-beta(DP) interface of F1-ATPase, and also contact the central gamma subunit. The inhibitor opens the catalytic interface between the alpha(DP) and beta(DP) subunits relative to previous structures. The presence of ATP in the catalytic site of the beta(DP) subunit implies that the inhibited state represents a pre-hydrolysis step on the catalytic pathway of the enzyme.

PubMed: 12923572
DOI: 10.1038/NSB966

実験手法

X-RAY DIFFRACTION (2.8 Å)