ATP increases the affinity between MutS ATPase domains: Implications for ATP hydrolysis and conformational changes

Journal of Biological Chemistry

Volumn 279, Issue 42, 2004, Pages 43879-43885

  Lamers, Meindert H ^a,d   Georgijevic, Dubravka ^b   Lebbink, Joyce H ^a   Winterwerp, Herrie H K ^a   Agianian, Bogos ^c   De Wind, Niels ^b   Sixma, Titia K ^a  

^a NETHERLANDS CANCER INSTITUTE   (Netherlands)

^b LEIDEN UNIVERSITY MEDICAL CENTER   (Netherlands)

^c UTRECHT UNIVERSITY   (Netherlands)

^d UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; CRYSTALLOGRAPHY; CRYSTALS; DIMERS; DNA; ESCHERICHIA COLI;

MISMATCH RECOGNITION; MISMATCH REPAIR; MUTANTS; NUCLEOTIDES;

ENZYMES;

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; BACTERIAL ENZYME; MUTANT PROTEIN;

ARTICLE; BINDING AFFINITY; BINDING KINETICS; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; ENZYME ACTIVITY; ENZYME BINDING; ENZYME CONFORMATION; ENZYME STRUCTURE; MISMATCH REPAIR; MUTATION; NONHUMAN; NUCLEOTIDE BINDING SITE; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DOMAIN; ULTRACENTRIFUGATION;

ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; AMINO ACID SUBSTITUTION; BACTERIAL PROTEINS; BASE PAIR MISMATCH; CRYSTALLOGRAPHY, X-RAY; DNA-BINDING PROTEINS; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; MUTS DNA MISMATCH-BINDING PROTEIN; PROTEIN CONFORMATION; RECOMBINANT PROTEINS;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA;

EID: 6344226679     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M406380200     Document Type: Article

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