Structure and mechanism in site-specific recombination.
Three-dimensional structural information on the integrase family of site-specific recombinases has only recently become available, with the crystal structures of catalytic domains, full-length proteins and protein-DNA complexes of this family reported over the past two years. These results have led to a model for the overall architecture and active site stereochemistry of the recombination pathway that addresses a number of interesting mechanistic issues.
Department of Biochemistry and Biophysics, Johnson Research Foundation, University of Pennsylvania School of Medicine, 37th and Hamilton Walk, A602 Richards Building, Philadelphia, PA 19104-6089, USA.
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Gopaul
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Duyne
D001665:Binding Sites / Q000235:genetics; D004247:DNA / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D004254:DNA Nucleotidyltransferases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D019426:Integrases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D008957:Models, Genetic; D008958:Models, Molecular; D009690:Nucleic Acid Conformation; D011487:Protein Conformation; D045522:Recombinases; D011995:Recombination, Genetic; D013237:Stereoisomerism; D014443:Tyrosine / Q000737:chemistry; D014764:Viral Proteins
D045522:Recombinases; D014764:Viral Proteins; D014443:Tyrosine; D004247:DNA; C045073:Cre recombinase; D004254:DNA Nucleotidyltransferases; D019426:Integrases; C115006:integron integrase IntI1