Recombining the structures of HIV integrase, RuvC and RNase H.
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.
Yang
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Department of Molecular Biophysics and Biochemistry, Howard Hughes Medical Institute, Yale University, New Haven, CT 06520, USA.
Steitz
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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*
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; C069806:ruvC protein, E coli; D004254:DNA Nucleotidyltransferases; D019426:Integrases; D004706:Endodeoxyribonucleases; D016914:Ribonuclease H