6ZA9

Fo domain of Ovine ATP synthase

6ZA9 の概要

• エントリーDOI: 10.2210/pdb6za9/pdb
• 関連するPDBエントリー: 6TT7
• EMDBエントリー: 11127
• 分子名称: ATP synthase F(0) complex subunit C1, mitochondrial, ATP synthase subunit e, mitochondrial, 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE, ... (13 entities in total)
• 機能のキーワード: atp synthase, mitochondrial, respiratory chain, mammalian, membrane protein
• 由来する生物種: Ovis aries (Sheep); 詳細
• タンパク質・核酸の鎖数: 17
• 化学式量合計: 246558.51

構造登録者

Pinke, G.,Zhou, L.,Sazanov, L.A. (登録日: 2020-06-05, 公開日: 2020-09-23, 最終更新日: 2024-05-01)

主引用文献

Pinke, G.,Zhou, L.,Sazanov, L.A.
Cryo-EM structure of the entire mammalian F-type ATP synthase.
Nat.Struct.Mol.Biol., 27:1077-1085, 2020

PubMed Abstract: The majority of adenosine triphosphate (ATP) powering cellular processes in eukaryotes is produced by the mitochondrial F1Fo ATP synthase. Here, we present the atomic models of the membrane Fo domain and the entire mammalian (ovine) F1Fo, determined by cryo-electron microscopy. Subunits in the membrane domain are arranged in the 'proton translocation cluster' attached to the c-ring and a more distant 'hook apparatus' holding subunit e. Unexpectedly, this subunit is anchored to a lipid 'plug' capping the c-ring. We present a detailed proton translocation pathway in mammalian Fo and key inter-monomer contacts in F1Fo multimers. Cryo-EM maps of F1Fo exposed to calcium reveal a retracted subunit e and a disassembled c-ring, suggesting permeability transition pore opening. We propose a model for the permeability transition pore opening, whereby subunit e pulls the lipid plug out of the c-ring. Our structure will allow the design of drugs for many emerging applications in medicine.

PubMed: 32929284
DOI: 10.1038/s41594-020-0503-8

実験手法

ELECTRON MICROSCOPY (3.76 Å)