SERCA mutant E309Q binds two Ca2+ions but adopts a catalytically incompetent conformation

Author:

Clausen Johannes D12,Bublitz Maike1,Arnou Bertrand12,Montigny Cédric3,Jaxel Christine3,Møller Jesper Vuust12,Nissen Poul1,Andersen Jens Peter2,le Maire Marc3

Affiliation:

1. Department of Molecular Biology and Genetics, Centre for Membrane Pumps in Cells and Disease - PUMPKIN, Danish National Research Foundation, Aarhus University; Aarhus Denmark

2. Department of Biomedicine, Aarhus University; Aarhus Denmark

3. Unité Mixte de Recherche 8221, Commissariat à l'Energie Atomique (CEA), Université Paris-Sud and Centre National de la Recherche Scientifique (CNRS); CEA de Saclay Gif-sur-Yvette France

Publisher

Wiley

Subject

General Immunology and Microbiology,General Biochemistry, Genetics and Molecular Biology,Molecular Biology,General Neuroscience

Reference60 articles.

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2. Characterization of detergent-solubilized sarcoplasmic reticulum Ca2+-ATPase by high-performance liquid chromatography;Andersen;Biochemistry,1986

3. Functional consequences of alterations to Glu309, Glu771, and Asp800 in the Ca2+-ATPase of sarcoplasmic reticulum;Andersen;J Biol Chem,1992

4. Amino acids Asn796 and Thr799 of the Ca2+-ATPase of sarcoplasmic reticulum bind Ca2+ at different sites;Andersen;J Biol Chem,1994

5. In and out of the cation pumps: P-Type ATPase structure revisited;Bublitz;Curr Opin Struct Biol,2010

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