Abstract
The recently determined structures of the catalytic domains of HIV integrase, avian sarcoma virus integrase and the Mu transposase are strikingly similar to each other and also exhibit significant similarity to several nucleases. All these enzymes of cut polynucleotides, leaving 3'OH and 5'PO4 groups. The integrase and transposase also possess a strand-transfer activity that splices DNA. The structural similarities among members of this superfamily of polynucleotidyl transferases suggest that they share a similar mechanism of catalysis.
MeSH terms
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Bacterial Proteins / chemistry
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Bacteriophage mu / enzymology
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Bacteriophage mu / genetics
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Catalysis
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DNA / metabolism
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DNA Nucleotidyltransferases / chemistry*
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DNA Nucleotidyltransferases / genetics
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DNA Nucleotidyltransferases / metabolism
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Endodeoxyribonucleases / chemistry
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Escherichia coli / enzymology
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Escherichia coli Proteins*
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HIV-1 / enzymology
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HIV-1 / genetics
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Integrases
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Models, Molecular
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Protein Conformation*
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Retroviridae / enzymology*
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Retroviridae / genetics
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Retroviridae Proteins / chemistry*
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Retroviridae Proteins / genetics
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Retroviridae Proteins / metabolism
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Ribonuclease H / chemistry
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Sequence Homology, Amino Acid
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Thermus thermophilus / enzymology
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Transposases
Substances
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Bacterial Proteins
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Escherichia coli Proteins
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Retroviridae Proteins
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ruvC protein, E coli
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DNA
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DNA Nucleotidyltransferases
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Integrases
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Transposases
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Endodeoxyribonucleases
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Ribonuclease H