8F29

Yeast ATP synthase in conformation-1 at pH 6

これはPDB形式変換不可エントリーです。

8F29 の概要

• エントリーDOI: 10.2210/pdb8f29/pdb
• EMDBエントリー: 28809
• 分子名称: ATP synthase subunit 5, mitochondrial, ATP synthase protein 8, ATP synthase subunit a, ... (17 entities in total)
• 機能のキーワード: f-type atp synthase, yeast, mitochondrial, membrane protein
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast); 詳細
• タンパク質・核酸の鎖数: 27
• 化学式量合計: 555951.16

構造登録者

Sharma, S.,Patel, H.,Luo, M.,Mueller, D.M.,Liao, M. (登録日: 2022-11-07, 公開日: 2024-02-07, 最終更新日: 2024-05-01)

主引用文献

Sharma, S.,Luo, M.,Patel, H.,Mueller, D.M.,Liao, M.
Conformational ensemble of yeast ATP synthase at low pH reveals unique intermediates and plasticity in F 1 -F o coupling.
Nat.Struct.Mol.Biol., 31:657-666, 2024

PubMed Abstract: Mitochondrial adenosine triphosphate (ATP) synthase uses the proton gradient across the inner mitochondrial membrane to synthesize ATP. Structural and single molecule studies conducted mostly at neutral or basic pH have provided details of the reaction mechanism of ATP synthesis. However, pH of the mitochondrial matrix is slightly acidic during hypoxia and pH-dependent conformational changes in the ATP synthase have been reported. Here we use single-particle cryo-EM to analyze the conformational ensemble of the yeast (Saccharomyces cerevisiae) ATP synthase at pH 6. Of the four conformations resolved in this study, three are reaction intermediates. In addition to canonical catalytic dwell and binding dwell structures, we identify two unique conformations with nearly identical positions of the central rotor but different catalytic site conformations. These structures provide new insights into the catalytic mechanism of the ATP synthase and highlight elastic coupling between the catalytic and proton translocating domains.

PubMed: 38316880
DOI: 10.1038/s41594-024-01219-4

実験手法

ELECTRON MICROSCOPY (4 Å)