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

被引：1081

作者：

Doublié, S ^{[1
]}

Tabor, S ^{[1
]}

Long, AM ^{[1
]}

Richardson, CC ^{[1
]}

Ellenberger, T ^{[1
]}

机构：

[1] Harvard Univ, Sch Med, Dept Biol Chem & Mol Pharmacol, Boston, MA 02115 USA

来源：

NATURE | 1998年 / 391卷 / 6664期

关键词：

D O I：

10.1038/34593

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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 Angstrom 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.

引用

页码：251 / 258

页数：8

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