Article
Crystal structure of D351A and P312A mutant forms of the mammalian sarcoplasmic reticulum Ca(2+) -ATPase reveals key events in phosphorylation and Ca(2+) release.
The Journal of biological chemistry - 23 May 2008
Marchand Alexandre, Winther Anne-Marie Lund, Holm Peter Joakim, Olesen Claus, Montigny Cedric, Arnou Bertrand, Champeil Philippe, Clausen Johannes D, Vilsen Bente, Andersen Jens Peter, Nissen Poul, Jaxel Christine, Møller Jesper Vuust, le Maire Marc
Abstract excerpt
In recent years crystal structures of the sarcoplasmic reticulum Ca(2+)-ATPase (SERCA1a), stabilized in various conformations with nucleotide and phosphate analogs, have been obtained. However, structural analysis of mutant forms would also be valuable to address key mechanistic aspects. We have worked out a procedure for affinity purification of SERCA1a heterologously expressed in yeast cells, producing...
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