The average conformation at micromolar [Ca2+] of Ca 2+-ATPase with bound nucleotide differs from that adopted with the transition state analog ADP·AlFx or with AMPPCP under crystallization conditions at millimolar [Ca2+]

Journal of Biological Chemistry

Volumn 280, Issue 19, 2005, Pages 18745-18754

  Picard, Martin ^a   Toyoshima, Chikashi ^b   Champeil, Philippe ^a  

^a CNRS   (France)

^b UNIVERSITY OF TOKYO   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINETRIPHOSPHATE; CRYSTAL STRUCTURE; CRYSTALLIZATION; DETERGENTS; POSITIVE IONS;

MUTATIONS; PROTEINASE; SARCOPLASMIC RETICULUM; TRANSITION STATE COMPLEX;

CALCIUM COMPOUNDS;

ADENOSINE 5' O (3 THIOTRIPHOSPHATE); ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE (CALCIUM); BETA,GAMMA METHYLENEADENOSINE TRIPHOSPHATE; CALCIUM 45; CALCIUM ION; 5' ADENYLYL (BETA,GAMMA METHYLENE)DIPHOSPHONATE; 5'-ADENYLYL (BETA,GAMMA-METHYLENE)DIPHOSPHONATE; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; ALUMINUM; CALCIUM; DRUG DERIVATIVE; FLUORINE; FLUOROALUMINUM; ION; MAGNESIUM; PROTEINASE K; SARCOPLASMIC RETICULUM CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE;

ARTICLE; BINDING AFFINITY; CRYSTALLIZATION; ENZYME ACTIVITY; ENZYME PHOSPHORYLATION; ENZYME STRUCTURE; PRIORITY JOURNAL; PROTEIN DEGRADATION; SARCOPLASMIC RETICULUM; ANIMAL; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; DOSE RESPONSE; METABOLISM; PERFUSION; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN TERTIARY STRUCTURE; RABBIT; TIME;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; ALUMINUM; ANIMALS; BINDING SITES; CALCIUM; CALCIUM-TRANSPORTING ATPASES; CRYSTALLIZATION; DOSE-RESPONSE RELATIONSHIP, DRUG; ENDOPEPTIDASE K; FLUORINE; IONS; MAGNESIUM; MODELS, MOLECULAR; PERFUSION; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; RABBITS; SARCOPLASMIC RETICULUM; SARCOPLASMIC RETICULUM CALCIUM-TRANSPORTING ATPASES; TIME FACTORS;

EID: 21444458507     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M501596200     Document Type: Article

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