6B2Z

Cryo-EM structure of the dimeric FO region of yeast mitochondrial ATP synthase

6B2Z の概要

• エントリーDOI: 10.2210/pdb6b2z/pdb
• 関連するPDBエントリー: 6B2Z 6B8H
• EMDBエントリー: 7036 7037 7067
• 分子名称: ATP synthase subunit c, mitochondrial, ATP synthase subunit k, mitochondrial, ATP synthase protein 8, ... (10 entities in total)
• 機能のキーワード: complex, dimer, mitochondrial inner membrane, proton translocation, membrane protein
• 由来する生物種: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); 詳細
• タンパク質・核酸の鎖数: 38
• 化学式量合計: 384616.64

構造登録者

Guo, H.,Rubinstein, J.L. (登録日: 2017-09-20, 公開日: 2017-11-08, 最終更新日: 2025-05-28)

主引用文献

Guo, H.,Bueler, S.A.,Rubinstein, J.L.
Atomic model for the dimeric FO region of mitochondrial ATP synthase.
Science, 358:936-940, 2017

PubMed Abstract: Mitochondrial adenosine triphosphate (ATP) synthase produces the majority of ATP in eukaryotic cells, and its dimerization is necessary to create the inner membrane folds, or cristae, characteristic of mitochondria. Proton translocation through the membrane-embedded F region turns the rotor that drives ATP synthesis in the soluble F region. Although crystal structures of the F region have illustrated how this rotation leads to ATP synthesis, understanding how proton translocation produces the rotation has been impeded by the lack of an experimental atomic model for the F region. Using cryo-electron microscopy, we determined the structure of the dimeric F complex from at a resolution of 3.6 angstroms. The structure clarifies how the protons travel through the complex, how the complex dimerizes, and how the dimers bend the membrane to produce cristae.

PubMed: 29074581
DOI: 10.1126/science.aao4815

実験手法

ELECTRON MICROSCOPY (3.6 Å)