Structural basis of ion pumping by Ca2+-ATPase of sarcoplasmic reticulum

被引：53

作者：

Toyoshima, C ^{[1
]}

Nomura, H ^{[1
]}

Sugita, Y ^{[1
]}

机构：

[1] Univ Tokyo, Inst Mol & Cellular Biosci, Bunkyo Ku, Tokyo 1130032, Japan

来源：

FEBS LETTERS | 2003年 / 555卷 / 01期

关键词：

crystal structure; ion pump; Ca2+-ATPase; SERCA1a; Ca2+ binding; domain movement;

D O I：

10.1016/S0014-5793(03)01086-X

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

The structures of the Ca2+-ATPase (SERCA1a) have been determined for five different states by X-ray crystallography. Detailed comparison of the structures in the Ca2+-bound form and unbound (but thapsigargin-bound) form reveals that very large rearrangements of the transmembrane helices take place accompanying Ca2+ dissociation and binding and that they are mechanically linked with equally large movements of the cytoplasmic domains. The meanings of the rearrangements of the transmembrane helices and those of the cytoplasmic domains, and the mechanistic roles of the phosphorylation are now becoming clear. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：106 / 110

页数：5

共 10 条

[1]

Organization of cytoplasmic domains of sarcoplasmic reticulum Ca2+-ATPase in E1P and E1ATP states:: a limited proteolysis study [J].