Dephosphorylation of the calcium pump coupled to counterion occlusion

Science

Volumn 306, Issue 5705, 2004, Pages 2251-2255

  Olesen, Claus ^a   Sørensen, Thomas Lykke Møller ^a   Nielsen, Rikke Christina ^a   Møller, Jesper Vuust ^a   Nissen, Poul ^a  

^a AARHUS UNIVERSITY   (Denmark)

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; CRYSTAL STRUCTURE; ENZYMES; HYDROLYSIS; PROTONS; PUMPS; REACTION KINETICS;

ADENOSINE TRIPHOSPHATE (ATP); ALUMINIUM FLUORIDE; CATION PUMPS; PHOSPHORYLATION;

CALCIUM;

ADENOSINE TRIPHOSPHATASE (CALCIUM); ADENOSINE TRIPHOSPHATE; ALUMINUM FLUORIDE; CALCIUM; HYDROGEN;

CHEMISTRY;

ARTICLE; CALCIUM TRANSPORT; CRYSTAL STRUCTURE; DEPHOSPHORYLATION; ENERGY; HYDROLYSIS; NONHUMAN; PHASE TRANSITION; PRIORITY JOURNAL; PROTEIN MOTIF; PROTEIN STRUCTURE; PROTEIN TRANSPORT; PROTON TRANSPORT; RABBIT; SARCOPLASMIC RETICULUM;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ALUMINUM COMPOUNDS; AMINO ACID MOTIFS; ANIMALS; BINDING SITES; BIOLOGICAL TRANSPORT, ACTIVE; CALCIUM; CALCIUM-TRANSPORTING ATPASES; CHEMISTRY, PHYSICAL; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; CYTOPLASM; FLUORIDES; HYDROLYSIS; ION TRANSPORT; MODELS, CHEMICAL; MODELS, MOLECULAR; PHOSPHORYLATION; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; PROTONS; RABBITS; SARCOPLASMIC RETICULUM; THAPSIGARGIN; THERMODYNAMICS;

ORYCTOLAGUS CUNICULUS;

EID: 11144330054     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.1106289     Document Type: Article

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29. We thank B. Holm, B. Nielsen, and C. Lauridsen for expert technical assistance; the staff at the Protein Structure Factory beamline BL14.1 of Free University Berlin at Berliner Elektronenspeicherring-Gesellschaft für Synchrotronstrahlung m. b. H., the staff at European Synchrotron Radiation Facility (ESRF) beamline ID29; J. L. Karlsen and R. Jørgensen for extensive computer support and J. Nyborg for fruitful scientific discussions. This work was supported by an Ole Rømer Research grant; the Center for Structural Biology; the Dansync program under the Danish Natural Science Research Council; 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 code 1XP5.