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Crystal Structures of Ca 2+ ‐ATPase in Various Physiological States
Author(s) -
TOYOSHIMA CHIKASHI,
NOMURA HIROMI,
SUGITA YUJI
Publication year - 2003
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.2003.tb07131.x
Subject(s) - chemistry , transmembrane domain , crystallography , atpase , thapsigargin , cytoplasm , crystal structure , transmembrane protein , dissociation (chemistry) , biophysics , stereochemistry , membrane , biochemistry , extracellular , biology , enzyme , receptor
A bstract : The structures of the Ca 2+ ‐ATPase (SERCA1a) in different physiological states were determined by X‐ray crystallography. Detailed comparison of the structures in the Ca 2+ ‐bound form and unbound (but thapsigargin bound) form reveals that very large rearrangements of the transmembrane helices take place accompanying Ca 2+ dissociation and binding and that they are mechanically linked with equally large movements of the cytoplasmic domains. The meaning of the rearrangement of the transmembrane helices becomes apparent by homology modeling of the Na + K + ‐ATPase.