6M0R

2.7A Yeast Vo state3

6M0R の概要

• エントリーDOI: 10.2210/pdb6m0r/pdb
• EMDBエントリー: 30034
• 分子名称: V-type proton ATPase subunit c', 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine, PYROPHOSPHATE, ... (13 entities in total)
• 機能のキーワード: v-atpase, vo sub-complex, cryoem, transport 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: 15
• 化学式量合計: 346827.82

構造登録者

Roh, S.H.,Shekhar, M.,Pintilie, G.,Chipot, C.,Wilkens, S.,Singharoy, A.,Chiu, W. (登録日: 2020-02-22, 公開日: 2020-11-04, 最終更新日: 2025-07-02)

主引用文献

Roh, S.H.,Shekhar, M.,Pintilie, G.,Chipot, C.,Wilkens, S.,Singharoy, A.,Chiu, W.
Cryo-EM and MD infer water-mediated proton transport and autoinhibition mechanisms of V o complex.
Sci Adv, 6:-, 2020

PubMed Abstract: Rotary vacuolar adenosine triphosphatases (V-ATPases) drive transmembrane proton transport through a V proton channel subcomplex. Despite recent high-resolution structures of several rotary ATPases, the dynamic mechanism of proton pumping remains elusive. Here, we determined a 2.7-Å cryo-electron microscopy (cryo-EM) structure of yeast V proton channel in nanodisc that reveals the location of ordered water molecules along the proton path, details of specific protein-lipid interactions, and the architecture of the membrane scaffold protein. Moreover, we uncover a state of V that shows the -ring rotated by ~14°. Molecular dynamics simulations demonstrate that the two rotary states are in thermal equilibrium and depict how the protonation state of essential glutamic acid residues couples water-mediated proton transfer with -ring rotation. Our cryo-EM models and simulations also rationalize a mechanism for inhibition of passive proton transport as observed for free V that is generated as a result of V-ATPase regulation by reversible disassembly in vivo.

PubMed: 33028525
DOI: 10.1126/sciadv.abb9605

実験手法

ELECTRON MICROSCOPY (2.7 Å)