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

FEBS Letters

Sugita, Yuji¹  Nomura, Hiromi¹  Toyoshima, Chikashi¹ 

[1] Institute of Molecular and Cellular Biosciences, The University of Tokyo, Bunkyo-ku, Tokyo 113-0032, Japan

关键词: Crystal structure;    Ion pump;    Ca2+-ATPase;    SERCA1a;    Ca2+ binding;    Domain movement;   

DOI  :  10.1016/S0014-5793(03)01086-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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.

【 授权许可】

Unknown