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

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 a...

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Bibliographic Details
Published inFEBS letters Vol. 555; no. 1; pp. 106 - 110
Main Authors Toyoshima, Chikashi, Nomura, Hiromi, Sugita, Yuji
Format Journal Article
LanguageEnglish
Japanese
Published 27.11.2003
Subjects
Ca2+ binding
Ca2+-ATPase
Crystal structure
Domain movement
Ion pump
SERCA1a
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Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(03)01086-X