Abstract
DNA polymerases change their specificity for nucleotide substrates with each catalytic cycle, while achieving error frequencies in the range of 10(-5) to 10(-6). Here we present a 2.2 A crystal structure of the replicative DNA polymerase from bacteriophage T7 complexed with a primer-template and a nucleoside triphosphate in the polymerase active site. The structure illustrates how nucleotides are selected in a template-directed manner, and provides a structural basis for a metal-assisted mechanism of phosphoryl transfer by a large group of related polymerases.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Bacteriophage T7 / chemistry*
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Binding Sites
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DNA, Bacterial / biosynthesis
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DNA, Bacterial / chemistry
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DNA, Bacterial / metabolism
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DNA-Directed DNA Polymerase / chemistry*
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DNA-Directed DNA Polymerase / metabolism
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Escherichia coli / genetics
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Escherichia coli / metabolism
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Metals / chemistry
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Metals / metabolism
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Models, Molecular
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Nucleic Acid Conformation
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Protein Conformation
Substances
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DNA, Bacterial
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Metals
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bacteriophage T7 induced DNA polymerase
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DNA-Directed DNA Polymerase