5D80

Crystal Structure of Yeast V1-ATPase in the Autoinhibited Form

5D80 の概要

• エントリーDOI: 10.2210/pdb5d80/pdb
• 関連するPDBエントリー: 5bw9
• 分子名称: V-type proton ATPase catalytic subunit A, V-type proton ATPase subunit B, V-type proton ATPase subunit H, ... (7 entities in total)
• 機能のキーワード: hydrolase, autoinhibition
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast); 詳細
• タンパク質・核酸の鎖数: 30
• 化学式量合計: 1189527.23

構造登録者

Oot, R.A.,Kane, P.M.,Berry, E.A.,Wilkens, S. (登録日: 2015-08-14, 公開日: 2016-06-08, 最終更新日: 2023-09-27)

主引用文献

Oot, R.A.,Kane, P.M.,Berry, E.A.,Wilkens, S.
Crystal structure of yeast V1-ATPase in the autoinhibited state.
Embo J., 35:1694-1706, 2016

PubMed Abstract: Vacuolar ATPases (V-ATPases) are essential proton pumps that acidify the lumen of subcellular organelles in all eukaryotic cells and the extracellular space in some tissues. V-ATPase activity is regulated by a unique mechanism referred to as reversible disassembly, wherein the soluble catalytic sector, V1, is released from the membrane and its MgATPase activity silenced. The crystal structure of yeast V1 presented here shows that activity silencing involves a large conformational change of subunit H, with its C-terminal domain rotating ~150° from a position near the membrane in holo V-ATPase to a position at the bottom of V1 near an open catalytic site. Together with biochemical data, the structure supports a mechanistic model wherein subunit H inhibits ATPase activity by stabilizing an open catalytic site that results in tight binding of inhibitory ADP at another site.

PubMed: 27295975
DOI: 10.15252/embj.201593447

実験手法

X-RAY DIFFRACTION (6.202 Å)