Dimerization of Escherichia coli DNA-gyrase B provides a structural mechanism for activating the ATPase catalytic center

Journal of Biological Chemistry

Volumn 275, Issue 13, 2000, Pages 9468-9475

  Brino, Laurent ^a   Urzhumtsev, Alexandre ^b   Mousli, Marc ^a,c   Bronner, Christian ^a,c   Mitschler, André ^a   Oudet, Pierre ^a   Moras, Dino ^a  

^a INSTITUT DE GÉNÉTIQUE ET DE BIOLOGIE MOLÉCULAIRE ET CELLULAIRE   (France)

^b Nancy University CNRS   (France)

^c INSERM   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; ADENYLYLIMIDODIPHOSPHATE; DNA; DNA TOPOISOMERASE (ATP HYDROLYSING); MAGNESIUM ION;

AMINO TERMINAL SEQUENCE; ARTICLE; DIMERIZATION; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME SUBUNIT; ESCHERICHIA COLI; HYDROLYSIS; HYDROPHOBICITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING;

ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; BINDING SITES; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; DNA GYRASE; DNA TOPOISOMERASES, TYPE II; ENZYME ACTIVATION; ESCHERICHIA COLI; HYDROLYSIS; ISOLEUCINE; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; TYROSINE;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0034737716     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.275.13.9468     Document Type: Article

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