6R10

Thermus thermophilus V/A-type ATPase/synthase, rotational state 1R

6R10 の概要

• エントリーDOI: 10.2210/pdb6r10/pdb
• 関連するPDBエントリー: 6QUM 6R0W 6R0Y 6R0Z
• EMDBエントリー: 4640 4699 4700 4702 4703
• 分子名称: V-type ATP synthase alpha chain, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (11 entities in total)
• 機能のキーワード: atp hydrolysis/synthesis, proton translocation, rotary catalysis, membrane protein
• 由来する生物種: Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579); 詳細
• タンパク質・核酸の鎖数: 26
• 化学式量合計: 681544.64

構造登録者

Zhou, L.,Sazanov, L. (登録日: 2019-03-13, 公開日: 2019-08-28, 最終更新日: 2024-05-15)

主引用文献

Zhou, L.,Sazanov, L.A.
Structure and conformational plasticity of the intact Thermus thermophilus V/A-type ATPase.
Science, 365:-, 2019

PubMed Abstract: V (vacuolar)/A (archaeal)-type adenosine triphosphatases (ATPases), found in archaea and eubacteria, couple ATP hydrolysis or synthesis to proton translocation across the plasma membrane using the rotary-catalysis mechanism. They belong to the V-type ATPase family, which differs from the mitochondrial/chloroplast F-type ATP synthases in overall architecture. We solved cryo-electron microscopy structures of the intact V/A-ATPase, reconstituted into lipid nanodiscs, in three rotational states and two substates. These structures indicate substantial flexibility between V and V in a working enzyme, which results from mechanical competition between central shaft rotation and resistance from the peripheral stalks. We also describe details of adenosine diphosphate inhibition release, V-V torque transmission, and proton translocation, which are relevant for the entire V-type ATPase family.

PubMed: 31439765
DOI: 10.1126/science.aaw9144

実験手法

ELECTRON MICROSCOPY (4.3 Å)