3RRK

Crystal structure of the cytoplasmic N-terminal domain of subunit I, homolog of subunit a, of V-ATPase

3RRK の概要

• エントリーDOI: 10.2210/pdb3rrk/pdb
• 分子名称: V-type ATPase 116 kDa subunit, 2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: alpha beta fold, proton pump, subunit i/a, v-atpase, proton transport
• 由来する生物種: Meiothermus ruber
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 39410.98

構造登録者

Srinivasan, S.,Vyas, N.K.,Baker, M.L.,Quiocho, F.A. (登録日: 2011-04-29, 公開日: 2011-08-10, 最終更新日: 2024-04-03)

主引用文献

Srinivasan, S.,Vyas, N.K.,Baker, M.L.,Quiocho, F.A.
Crystal structure of the cytoplasmic N-terminal domain of subunit I, a homolog of subunit a, of V-ATPase.
J.Mol.Biol., 412:14-21, 2011

PubMed Abstract: Subunit "a" is associated with the membrane-bound (V(O)) complex of eukaryotic vacuolar H(+)-ATPase acidification machinery. It has also been shown recently to be involved in diverse membrane fusion/secretory functions independent of acidification. Here, we report the crystal structure of the N-terminal cytosolic domain from the Meiothermus ruber subunit "I" homolog of subunit a. The structure is composed of a curved long central α-helix bundle capped on both ends by two lobes with similar α/β architecture. Based on the structure, a reasonable model of its eukaryotic subunit a counterpart was obtained. The crystal structure and model fit well into reconstructions from electron microscopy of prokaryotic and eukaryotic vacuolar H(+)-ATPases, respectively, clarifying their orientations and interactions and revealing features that could enable subunit a to play a role in membrane fusion/secretion.

PubMed: 21787787
DOI: 10.1016/j.jmb.2011.07.014

実験手法

X-RAY DIFFRACTION (2.64 Å)