Crystal structure of a wild-type Cre recombinase-IoxP synapse reveals a novel spacer conformation suggesting an alternative mechanism for DNA cleavage activation

Nucleic Acids Research

Volumn 31, Issue 18, 2003, Pages 5449-5460

  Ennifar, Eric ^b   Meyer, Joachim E W ^b,c   Buchholz, Frank ^a   Stewart, A Francis ^a   Suck, Dietrich ^b  

^a DRESDEN UNIVERSITY OF TECHNOLOGY   (Germany)

^b EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^c Axaron Bioscience AG   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CRE RECOMBINASE; PHOSPHODIESTERASE; PHOSPHOROTHIOIC ACID; PROTEIN TYROSINE PHOSPHATASE; SPACER DNA; TETRAMER;

ARTICLE; BACTERIOPHAGE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; COVALENT BOND; CRYSTAL STRUCTURE; DNA CLEAVAGE; DNA CONFORMATION; DNA HELIX; DNA MODIFICATION; DNA PROTEIN COMPLEX; DNA STRAND BREAKAGE; DNA STRUCTURE; DNA TRANSFER; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME SUBUNIT; ESCHERICHIA COLI; GENE CONVERSION; GENE INTERACTION; GENE REARRANGEMENT; GENETIC RECOMBINATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DNA INTERACTION; WILD TYPE;

BASE SEQUENCE; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; DNA; INTEGRASES; MODELS, MOLECULAR; NUCLEIC ACID CONFORMATION; OLIGONUCLEOTIDES; PROTEIN BINDING; PROTEIN CONFORMATION; RECOMBINATION, GENETIC; THIONUCLEOTIDES; VIRAL PROTEINS;

ESCHERICHIA COLI; NEGIBACTERIA; UNIDENTIFIED BACTERIOPHAGE;

EID: 0344012172     PISSN: 03051048     EISSN: None     Source Type: Journal    
DOI: 10.1093/nar/gkg732     Document Type: Article

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