6C6L

Yeast Vacuolar ATPase Vo in lipid nanodisc

6C6L の概要

• エントリーDOI: 10.2210/pdb6c6l/pdb
• EMDBエントリー: 7348
• 分子名称: V-type proton ATPase subunit c', V-type proton ATPase subunit c'', V0 assembly protein 1, ... (8 entities in total)
• 機能のキーワード: vacuolar h+-atpase, vo proton channel, rotary motor enzyme, membrane 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: 353416.86

構造登録者

Roh, S.,Stam, N.J.,Hryc, C.,Couoh-Cardel, S.,Pintilie, G.,Chiu, W.,Wilkens, S. (登録日: 2018-01-19, 公開日: 2018-03-21, 最終更新日: 2024-03-13)

主引用文献

Roh, S.H.,Stam, N.J.,Hryc, C.F.,Couoh-Cardel, S.,Pintilie, G.,Chiu, W.,Wilkens, S.
The 3.5- angstrom CryoEM Structure of Nanodisc-Reconstituted Yeast Vacuolar ATPase VoProton Channel.
Mol. Cell, 69:993-1004.e3, 2018

PubMed Abstract: The molecular mechanism of transmembrane proton translocation in rotary motor ATPases is not fully understood. Here, we report the 3.5-Å resolution cryoEM structure of the lipid nanodisc-reconstituted V proton channel of the yeast vacuolar H-ATPase, captured in a physiologically relevant, autoinhibited state. The resulting atomic model provides structural detail for the amino acids that constitute the proton pathway at the interface of the proteolipid ring and subunit a. Based on the structure and previous mutagenesis studies, we propose the chemical basis of transmembrane proton transport. Moreover, we discovered that the C terminus of the assembly factor Voa1 is an integral component of mature V. Voa1's C-terminal transmembrane α helix is bound inside the proteolipid ring, where it contributes to the stability of the complex. Our structure rationalizes possible mechanisms by which mutations in human V can result in disease phenotypes and may thus provide new avenues for therapeutic interventions.

PubMed: 29526695
DOI: 10.1016/j.molcel.2018.02.006

実験手法

ELECTRON MICROSCOPY (3.5 Å)