| Literature DB >> 12161745 |
Alexander C Drohat1, Keehwan Kwon, Daniel J Krosky, James T Stivers.
Abstract
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.Entities:
Mesh：
Substances：
Year: 2002 PMID： 12161745 DOI： 10.1038/nsb829
Source DB: PubMed Journal: Nat Struct Biol ISSN： 1072-8368