6PE4

Yeast Vo motor in complex with 1 VopQ molecule

6PE4 の概要

• エントリーDOI: 10.2210/pdb6pe4/pdb
• EMDBエントリー: 20322
• 分子名称: V-type proton ATPase subunit a, vacuolar isoform, V0 assembly protein 1, V-type proton ATPase subunit d, ... (9 entities in total)
• 機能のキーワード: complex, transport protein
• 由来する生物種: Vibrio parahaemolyticus; 詳細
• タンパク質・核酸の鎖数: 16
• 化学式量合計: 428342.07

構造登録者

Peng, W.,Li, Y.,Tomchick, D.R.,Orth, K. (登録日: 2019-06-20, 公開日: 2020-05-20, 最終更新日: 2024-03-20)

主引用文献

Peng, W.,Casey, A.K.,Fernandez, J.,Carpinone, E.M.,Servage, K.A.,Chen, Z.,Li, Y.,Tomchick, D.R.,Starai, V.J.,Orth, K.
A distinct inhibitory mechanism of the V-ATPase by Vibrio VopQ revealed by cryo-EM.
Nat.Struct.Mol.Biol., 27:589-597, 2020

PubMed Abstract: The Vibrio parahaemolyticus T3SS effector VopQ targets host-cell V-ATPase, resulting in blockage of autophagic flux and neutralization of acidic compartments. Here, we report the cryo-EM structure of VopQ bound to the V subcomplex of the V-ATPase. VopQ inserts into membranes and forms an unconventional pore while binding directly to subunit c of the V-ATPase membrane-embedded subcomplex V. We show that VopQ arrests yeast growth in vivo by targeting the immature V subcomplex in the endoplasmic reticulum (ER), thus providing insight into the observation that VopQ kills cells in the absence of a functional V-ATPase. VopQ is a bacterial effector that has been discovered to inhibit a host-membrane megadalton complex by coincidentally binding its target, inserting into a membrane and disrupting membrane potential. Collectively, our results reveal a mechanism by which bacterial effectors modulate host cell biology and provide an invaluable tool for future studies on V-ATPase-mediated membrane fusion and autophagy.

PubMed: 32424347
DOI: 10.1038/s41594-020-0429-1

実験手法

ELECTRON MICROSCOPY (3.1 Å)