Structural basis for proofreading during replication of the Escherichia coli chromosome

被引：122

作者：

Hamdan, S ^{[1
]}

Carr, PD ^{[1
]}

Brown, SE ^{[1
]}

Ollis, DL ^{[1
]}

Dixon, NE ^{[1
]}

机构：

[1] Australian Natl Univ, Res Sch Chem, Canberra, ACT 0200, Australia

来源：

STRUCTURE | 2002年 / 10卷 / 04期

基金：

澳大利亚研究理事会;

关键词：

binuclear metallohydrolase; DNA polymerase III; DnaQ; DNA replication; exonuclease (3 '-5 '); manganese metalloenzyme; X-ray crystallography;

D O I：

10.1016/S0969-2126(02)00738-4

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The epsilon subunit of the Escherichia coli replicative DNA polymerase III is the proofreading 3'-5' exonuclease. Structures of its catalytic N-terminal domain (086) were determined at two pH values (5.8 and 8.5) at resolutions of 1.7-1.8 Angstrom, in complex with two Mn(II) ions and a nucleotide product of its reaction, thymidine 5'-monophosphate. The protein structure is built around a core five-stranded beta sheet that is a common feature of members of the DnaQ superfamily. The structures were identical, except for differences in the way TMP and water molecules are coordinated to the binuclear metal center in the active site. These data are used to develop a mechanism for epsilon and to produce a plausible model of the complex of epsilon186 with DNA.

引用

页码：535 / 546

页数：12

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