title: Recombining the structures of HIV integrase, RuvC and RNase H.
abstract: The recently reported crystal structures of two recombination enzymes, the catalytic domain of HIV integrase and Escherichia coli RuvC, an endonuclease, are surprisingly similar to that of ribonuclease H suggesting the possibility that they have a common enzymatic mechanism.
authors.affiliation: Department of Molecular Biophysics and Biochemistry, Howard Hughes Medical Institute, Yale University, New Haven, CT 06520, USA.
authors.forename: W
authors.initials: W
authors.lastname: Yang
authors.forename: T A
authors.initials: TA
authors.lastname: Steitz
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D004254:DNA Nucleotidyltransferases / Q000737:chemistry*; D004706:Endodeoxyribonucleases / Q000737:chemistry*; D004926:Escherichia coli / Q000201:enzymology; D029968:Escherichia coli Proteins; D006678:HIV / Q000201:enzymology*; D006801:Humans; D019426:Integrases; D017433:Protein Structure, Secondary; D011995:Recombination, Genetic / Q000235:genetics; D016914:Ribonuclease H / Q000737:chemistry*; D016662:Virus Integration / Q000502:physiology*
chemical_list: D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; C069806:ruvC protein, E coli; D004254:DNA Nucleotidyltransferases; D019426:Integrases; D004706:Endodeoxyribonucleases; D016914:Ribonuclease H