5ARA

Bovine mitochondrial ATP synthase state 1a

5ARA の概要

• エントリーDOI: 10.2210/pdb5ara/pdb
• 関連するPDBエントリー: 5ARE 5ARH 5ARI 5FIJ 5FIK 5FIL
• EMDBエントリー: 3164
• 分子名称: ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL, ATP SYNTHASE-COUPLING FACTOR 6, MITOCHONDRIAL, ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL, ... (11 entities in total)
• 機能のキーワード: hydrolase, atp synthase, rotary atpase
• 由来する生物種: BOS TAURUS (COW); 詳細
• 細胞内の位置: Mitochondrion inner membrane : P19483; Mitochondrion: P02721 P00829 P05631 P05630 P05632 P13621 P13619 P13620; Mitochondrion inner membrane; Multi-pass membrane protein: P00847; Mitochondrion membrane; Multi-pass membrane protein: P32876
• タンパク質・核酸の鎖数: 22
• 化学式量合計: 518892.57

構造登録者

Zhou, A.,Rohou, A.,Schep, D.G.,Bason, J.V.,Montgomery, M.G.,Walker, J.E.,Grigorieff, N.,Rubinstein, J.L. (登録日: 2015-09-24, 公開日: 2015-10-14, 最終更新日: 2024-05-08)

主引用文献

Zhou, A.,Rohou, A.,Schep, D.G.,Bason, J.V.,Montgomery, M.G.,Walker, J.E.,Grigorieff, N.,Rubinstein, J.L.
Structure and conformational states of the bovine mitochondrial ATP synthase by cryo-EM.
Elife, 4:e10180-e10180, 2015

PubMed Abstract: Adenosine triphosphate (ATP), the chemical energy currency of biology, is synthesized in eukaryotic cells primarily by the mitochondrial ATP synthase. ATP synthases operate by a rotary catalytic mechanism where proton translocation through the membrane-inserted FO region is coupled to ATP synthesis in the catalytic F1 region via rotation of a central rotor subcomplex. We report here single particle electron cryomicroscopy (cryo-EM) analysis of the bovine mitochondrial ATP synthase. Combining cryo-EM data with bioinformatic analysis allowed us to determine the fold of the a subunit, suggesting a proton translocation path through the FO region that involves both the a and b subunits. 3D classification of images revealed seven distinct states of the enzyme that show different modes of bending and twisting in the intact ATP synthase. Rotational fluctuations of the c8-ring within the FO region support a Brownian ratchet mechanism for proton-translocation-driven rotation in ATP synthases.

PubMed: 26439008
DOI: 10.7554/eLife.10180

実験手法

ELECTRON MICROSCOPY (7.4 Å)