3FKS

Yeast F1 ATPase in the absence of bound nucleotides

3FKS の概要

• エントリーDOI: 10.2210/pdb3fks/pdb
• 関連するPDBエントリー: 1W0J 2HLD
• 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: atp synthase, atp phosphatase, f1f0 atpase, atp synthesis, atp-binding, cf(1), hydrogen ion transport, ion transport, membrane, mitochondrion, mitochondrion inner membrane, nucleotide-binding, phosphoprotein, transport, hydrolase
• 由来する生物種: Saccharomyces cerevisiae (yeast); 詳細
• 細胞内の位置: Mitochondrion inner membrane : P07251; Mitochondrion: P00830 P38077 Q12165 P21306
• タンパク質・核酸の鎖数: 27
• 化学式量合計: 1120103.58

構造登録者

Kabaleeswaran, V.,Symersky, J.,Shen, H.,Walker, J.E.,Leslie, A.G.W.,Mueller, D.M. (登録日: 2008-12-17, 公開日: 2009-03-03, 最終更新日: 2023-09-06)

主引用文献

Kabaleeswaran, V.,Shen, H.,Symersky, J.,Walker, J.E.,Leslie, A.G.,Mueller, D.M.
Asymmetric structure of the yeast f1 ATPase in the absence of bound nucleotides.
J.Biol.Chem., 284:10546-10551, 2009

PubMed Abstract: The crystal structure of nucleotide-free yeast F(1) ATPase has been determined at a resolution of 3.6 A. The overall structure is very similar to that of the ground state enzyme. In particular, the beta(DP) and beta(TP) subunits both adopt the closed conformation found in the ground state structure despite the absence of bound nucleotides. This implies that interactions between the gamma and beta subunits are as important as nucleotide occupancy in determining the conformational state of the beta subunits. Furthermore, this result suggests that for the mitochondrial enzyme, there is no state of nucleotide occupancy that would result in more than one of the beta subunits adopting the open conformation. The adenine-binding pocket of the beta(TP) subunit is disrupted in the apoenzyme, suggesting that the beta(DP) subunit is responsible for unisite catalytic activity.

PubMed: 19233840
DOI: 10.1074/jbc.M900544200

実験手法

X-RAY DIFFRACTION (3.587 Å)