4DL0

Crystal Structure of the heterotrimeric EGChead Peripheral Stalk Complex of the Yeast Vacuolar ATPase

4DL0 の概要

• エントリーDOI: 10.2210/pdb4dl0/pdb
• 分子名称: V-type proton ATPase subunit C, V-type proton ATPase subunit G, V-type proton ATPase subunit E, ... (6 entities in total)
• 機能のキーワード: coiled-coil, heterotrimer, peripheral stalk, stator complex, hydrolase, ion transport, vacuolar atpase, vacuolar membrane
• 由来する生物種: Saccharomyces cerevisiae (yeast); 詳細
• 細胞内の位置: Vacuole membrane ; Peripheral membrane protein : P31412 P22203
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 109899.44

構造登録者

Oot, R.A.,Huang, L.S.,Berry, E.A.,Wilkens, S. (登録日: 2012-02-05, 公開日: 2012-10-10, 最終更新日: 2024-02-28)

主引用文献

Oot, R.A.,Huang, L.S.,Berry, E.A.,Wilkens, S.
Crystal Structure of the Yeast Vacuolar ATPase Heterotrimeric EGC(head) Peripheral Stalk Complex.
Structure, 20:1881-1892, 2012

PubMed Abstract: Vacuolar ATPases (V-ATPases) are multisubunit rotary motor proton pumps that function to acidify subcellular organelles in all eukaryotic organisms. V-ATPase is regulated by a unique mechanism that involves reversible dissociation into V₁-ATPase and V₀ proton channel, a process that involves breaking of protein interactions mediated by subunit C, the cytoplasmic domain of subunit "a" and three "peripheral stalks," each made of a heterodimer of E and G subunits. Here, we present crystal structures of a yeast V-ATPase heterotrimeric complex composed of EG heterodimer and the head domain of subunit C (C(head)). The structures show EG heterodimer folded in a noncanonical coiled coil that is stabilized at its N-terminal ends by binding to C(head). The coiled coil is disrupted by a bulge of partially unfolded secondary structure in subunit G and we speculate that this unique feature in the eukaryotic V-ATPase peripheral stalk may play an important role in enzyme structure and regulation by reversible dissociation.

PubMed: 23000382
DOI: 10.1016/j.str.2012.08.020

実験手法

X-RAY DIFFRACTION (2.905 Å)