6J54

Cryo-EM structure of the mammalian E-state ATP synthase FO section

6J54 の概要

• エントリーDOI: 10.2210/pdb6j54/pdb
• EMDBエントリー: 0668
• 分子名称: ATP synthase peripheral stalk-membrane subunit b, Mitochondrial H+ transporting ATP synthase subunit c isoform 1, ATP synthase membrane subunit 6.8PL, ... (11 entities in total)
• 機能のキーワード: membrane protein
• 由来する生物種: Sus scrofa (Pig); 詳細
• タンパク質・核酸の鎖数: 18
• 化学式量合計: 132628.78

構造登録者

Gu, J.,Zhang, L.,Yi, J.,Yang, M. (登録日: 2019-01-10, 公開日: 2019-06-26, 最終更新日: 2024-03-27)

主引用文献

Gu, J.,Zhang, L.,Zong, S.,Guo, R.,Liu, T.,Yi, J.,Wang, P.,Zhuo, W.,Yang, M.
Cryo-EM structure of the mammalian ATP synthase tetramer bound with inhibitory protein IF1.
Science, 364:1068-1075, 2019

PubMed Abstract: The mitochondrial adenosine triphosphate (ATP) synthase produces most of the ATP required by mammalian cells. We isolated porcine tetrameric ATP synthase and solved its structure at 6.2-angstrom resolution using a single-particle cryo-electron microscopy method. Two classical V-shaped ATP synthase dimers lie antiparallel to each other to form an H-shaped ATP synthase tetramer, as viewed from the matrix. ATP synthase inhibitory factor subunit 1 (IF1) is a well-known in vivo inhibitor of mammalian ATP synthase at low pH. Two IF1 dimers link two ATP synthase dimers, which is consistent with the ATP synthase tetramer adopting an inhibited state. Within the tetramer, we refined structures of intact ATP synthase in two different rotational conformations at 3.34- and 3.45-Å resolution.

PubMed: 31197009
DOI: 10.1126/science.aaw4852

実験手法

ELECTRON MICROSCOPY (3.94 Å)