Abstract
The crystal structure of the RuvC protein, a Holliday junction resolvase from E. coli, has been determined at 2.5 A resolution. The enzyme forms a dimer of 19 kDa subunits related by a dyad axis. Together with results from extensive mutational analyses, the refined structure reveals that the catalytic center, comprising four acidic residues, lies at the bottom of a cleft that nicely fits a DNA duplex. The structural features of the dimer, with a 30 A spacing between the two catalytic centers, provide a substantially defined image of the Holliday junction architecture. The folding topology in the vicinity of the catalytic site exhibits a striking similarity to that of RNAase H1 from E. coli.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Bacterial Proteins / chemistry*
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Base Sequence
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Binding Sites
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Computer Simulation
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Crystallography, X-Ray
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DNA, Bacterial / chemistry
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DNA, Bacterial / 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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Models, Molecular
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Molecular Sequence Data
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Nucleic Acid Conformation
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Nucleotidyltransferases / chemistry*
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Protein Conformation
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Recombination, Genetic
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Ribonuclease H / chemistry
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Transposases
Substances
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Bacterial Proteins
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DNA, Bacterial
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Escherichia coli Proteins
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ruvC protein, E coli
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Nucleotidyltransferases
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Transposases
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Endodeoxyribonucleases
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Ribonuclease H
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ribonuclease HI