Nature. 1998 Jan 15;391(6664):251-8.

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

Doublié S, Tabor S, Long AM, Richardson CC, Ellenberger T.

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Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115, USA.

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.

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Nature. 1998 Jan 15;391(6664):231-2.

PMID:: 9440688; [PubMed - indexed for MEDLINE]

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Structures reported by this article

T7 Dna Polymerase Complexed To Dna PrimerTEMPLATE,A Nucleoside Triphosphate, And Its Processivity Factor Thioredoxin

PDB: 1T7P

Source: Enterobacteria phage T7, Escherichia coli

Method: X-Ray Diffraction

Resolution: 2.2 Å

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

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