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

Sylvie Doublié; Stanley Tabor; Alexander M. Long; Charles C. Richardson; Tom Ellenberger

doi:10.1038/34593

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

Sylvie Doublié, Stanley Tabor, Alexander M. Long, Charles C. Richardson, Tom Ellenberger

Department of Biochemistry & Molecular Biophysics

Research output: Contribution to journal › Article › peer-review

1104 Scopus citations

Abstract

DNA polymerases change their specificity for nucleotide substrates with each catalytic cycle, while achieving error frequencies in the range of 10^- ⁶ to 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 polymeraae active site. The structure illustrate how nucleotides are selected in a template-directed manner, and provides a structural baals for a metal-assisted mechanism of phosphoryl transfer by a large group of related polymerases.

Original language	English
Pages (from-to)	251-258
Number of pages	8
Journal	Nature
Volume	391
Issue number	6664
DOIs	https://doi.org/10.1038/34593
State	Published - Jan 15 1998

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abstract = "DNA polymerases change their specificity for nucleotide substrates with each catalytic cycle, while achieving error frequencies in the range of 10- 6 to 10-6. Here we present a 2.2 {\AA} crystal structure of the replicative DNA polymerase from bacteriophage T7 complexed with a primer-template and a nucleoside triphosphate in the polymeraae active site. The structure illustrate how nucleotides are selected in a template-directed manner, and provides a structural baals for a metal-assisted mechanism of phosphoryl transfer by a large group of related polymerases.",

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AU - Doublié, Sylvie

AU - Tabor, Stanley

AU - Long, Alexander M.

AU - Richardson, Charles C.

AU - Ellenberger, Tom

PY - 1998/1/15

Y1 - 1998/1/15

N2 - DNA polymerases change their specificity for nucleotide substrates with each catalytic cycle, while achieving error frequencies in the range of 10- 6 to 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 polymeraae active site. The structure illustrate how nucleotides are selected in a template-directed manner, and provides a structural baals for a metal-assisted mechanism of phosphoryl transfer by a large group of related polymerases.

AB - DNA polymerases change their specificity for nucleotide substrates with each catalytic cycle, while achieving error frequencies in the range of 10- 6 to 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 polymeraae active site. The structure illustrate how nucleotides are selected in a template-directed manner, and provides a structural baals for a metal-assisted mechanism of phosphoryl transfer by a large group of related polymerases.

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JO - Nature

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

Abstract

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