5Y60

V/A-type ATPase/synthase from Thermus thermophilus, rotational state 3.

5Y60 の概要

• エントリーDOI: 10.2210/pdb5y60/pdb
• EMDBエントリー: 6813
• 分子名称: V-type ATP synthase alpha chain, ADENOSINE-5'-DIPHOSPHATE, V-type ATP synthase beta chain, ... (10 entities in total)
• 機能のキーワード: atp synthase, proton pump, v-atpase, bioenergetics, motor protein
• 由来する生物種: Thermus thermophilus HB8; 詳細
• タンパク質・核酸の鎖数: 26
• 化学式量合計: 681628.56

構造登録者

Nakanishi, A.,Kishikawa, J.,Tamakoshi, M.,Mitsuoka, K.,Yokoyama, K. (登録日: 2017-08-10, 公開日: 2018-01-17, 最終更新日: 2024-03-27)

主引用文献

Nakanishi, A.,Kishikawa, J.I.,Tamakoshi, M.,Mitsuoka, K.,Yokoyama, K.
Cryo EM structure of intact rotary H+-ATPase/synthase from Thermus thermophilus
Nat Commun, 9:89-89, 2018

PubMed Abstract: Proton translocating rotary ATPases couple ATP hydrolysis/synthesis, which occurs in the soluble domain, with proton flow through the membrane domain via a rotation of the common central rotor complex against the surrounding peripheral stator apparatus. Here, we present a large data set of single particle cryo-electron micrograph images of the V/A type H-rotary ATPase from the bacterium Thermus thermophilus, enabling the identification of three rotational states based on the orientation of the rotor subunit. Using masked refinement and classification with signal subtractions, we obtain homogeneous reconstructions for the whole complexes and soluble V domains. These reconstructions are of higher resolution than any EM map of intact rotary ATPase reported previously, providing a detailed molecular basis for how the rotary ATPase maintains structural integrity of the peripheral stator apparatus, and confirming the existence of a clear proton translocation path from both sides of the membrane.

PubMed: 29311594
DOI: 10.1038/s41467-017-02553-6

実験手法

ELECTRON MICROSCOPY (7.5 Å)