3-methyladenine DNA glycosylase I is an unexpected helix-hairpin-helix superfamily member

被引：48

作者：

Drohat, AC ^{[1
]}

Kwon, K ^{[1
]}

Krosky, DJ ^{[1
]}

Stivers, JT ^{[1
]}

机构：

[1] Johns Hopkins Univ, Sch Med, Dept Pharmacol & Mol Sci, Baltimore, MD 21205 USA

来源：

NATURE STRUCTURAL BIOLOGY | 2002年 / 9卷 / 09期

关键词：

D O I：

10.1038/nsb829

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 Escherichia coli enzyme 3-methyladenine DNA glycosylase I (TAG) hydrolyzes the glycosidic bond of 3-methyladenine (3-MeA) in DNA and is found in many bacteria and some higher eukaryotes. TAG shows little primary sequence identity with members of the well-known helix-hairpin-helix (HhH) superfamily of DNA repair glycosylases, which consists of AlkA, EndoIII, MutY and hOGG1. Unexpectedly, the three-dimensional solution structure reported here reveals TAG as member of this superfamily. The restricted specificity of TAG for 3-MeA bases probably arises from its unique aromatic rich 3-MeA binding pocket and the absence of a catalytic aspartate that is present in all other HhH family members.

引用

页码：659 / 664

页数：6

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