Crystal Structure of the Cytoplasmic N-Terminal Domain of Subunit I, a Homolog of Subunit a, of V-ATPase

被引：44

作者：

Srinivasan, Sankaranarayanan ^{[1
]}

Vyas, Nand K. ^{[1
]}

Baker, Matthew L. ^{[1
,2
]}

Quiocho, Florante A. ^{[1
]}

机构：

[1] Baylor Coll Med, Verna & Marrs McLean Dept Biochem & Mol Biol, Houston, TX 77030 USA

[2] Baylor Coll Med, Natl Ctr Macromol Imaging, Houston, TX 77030 USA

来源：

JOURNAL OF MOLECULAR BIOLOGY | 2011年 / 412卷 / 01期

基金：

美国国家卫生研究院;

关键词：

A/V-type ATPase; EM fit; membrane fusion/secretion; protein structure; proton pumping; H+-ATPASE; 3-DIMENSIONAL STRUCTURE; REVEALS; V-1; A1; SECRETION; INTERACTS; SYNTHASE; SECTOR; STALK;

D O I：

10.1016/j.jmb.2011.07.014

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 alpha-helix bundle capped on both ends by two lobes with similar alpha/beta 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. (C) 2011 Elsevier Ltd. All rights reserved.

引用

页码：14 / 21

页数：8

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