Phosphoryl transfer and calcium ion occlusion in the calcium pump

Science

Volumn 304, Issue 5677, 2004, Pages 1672-1675

  Sørensen, Thomas Lykke Moller ^a   Møller, Jesper Vuust ^a   Nissen, Poul ^a  

^a AARHUS UNIVERSITY   (Denmark)

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; CALCIUM; CONFORMATIONS; CRYSTAL STRUCTURE; HYDROLYSIS;

ION PUMPS; VECTORIAL ION TRANSPORT;

ADENOSINETRIPHOSPHATE;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATASE (CALCIUM); ADENOSINE TRIPHOSPHATE DERIVATIVE; ALUMINUM FLUORIDE; BETA,GAMMA METHYLENEADENOSINE TRIPHOSPHATE; CALCIUM ION;

ARTICLE; CALCIUM TRANSPORT; ENDOPLASMIC RETICULUM; ENZYME ACTIVITY; ENZYME PHOSPHORYLATION; MEMBRANE TRANSPORT; NONHUMAN; PRIORITY JOURNAL; SARCOPLASMIC RETICULUM;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ALUMINUM COMPOUNDS; ANIMALS; BINDING SITES; CALCIUM; CALCIUM-TRANSPORTING ATPASES; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; CYTOSOL; FLUORIDES; MODELS, MOLECULAR; MUSCLE FIBERS, FAST-TWITCH; PHOSPHORYLATION; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RABBITS; SARCOPLASMIC RETICULUM CALCIUM-TRANSPORTING ATPASES;

EID: 2942668632     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.1099366     Document Type: Article

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28. We thank B. Holm and C. Lauridsen for expert technical assistance; the staffs at the Protein Structure Factory at Berliner Elektronenspeicherring- Gesellschaft für Synchrotron Strahlung m.b.H., European Synchrotron Radiation Facility beamline ID29, and Deutsches Elektronen-Synchrotron (DESY/EMBL) beamline BW7B; R. C. Nielsen, C. Olesen, and S. Thirup for assistance in data collection; J. L. Karlsen for extensive computer support; and J. Nyborg for fruitful scientific discussions. Supported by an Ole Rømer Research grant, the Center for Structural Biology, the Dansync Program under the Danish Natural Science Research Council, the Young investigation Program of the European Molecular Biology Organization, a grant from the Lundbeck Foundation (P.N.), and grants from the Danish Medical Research Council, Aarhus University Research Foundation, and NOVO Nordic Foundation (J.V.M). Coordinates and structure-factor amplitudes have been deposited to the Protein Data Bank under codes 1T5S and 1T5T.