Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 Å resolution

Sylvie Doublié, Stanley Tabor, Alexander M. Long, Charles C. Richardson and Tom Ellenberger ()
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Sylvie Doublié: Harvard Medical School
Stanley Tabor: Harvard Medical School
Alexander M. Long: Harvard Medical School
Charles C. Richardson: Harvard Medical School
Tom Ellenberger: Harvard Medical School

Nature, 1998, vol. 391, issue 6664, 251-258

Abstract: Abstract DNA polymerases change their specificity for nucleotide substrates with each catalytic cycle, while achieving error frequencies in the range of 10−5to 10−6. Here we present a 2.2 Å 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.

Date: 1998
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DOI: 10.1038/34593

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