1lmz
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(New page: 200px<br /><applet load="1lmz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lmz" /> '''Solution Structure of 3-Methyladenine DNA Gl...)
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Revision as of 18:34, 20 November 2007
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Solution Structure of 3-Methyladenine DNA Glycosylase I (TAG)
Overview
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.
About this Structure
1LMZ is a Single protein structure of sequence from Escherichia coli. Active as DNA-3-methyladenine glycosylase I, with EC number 3.2.2.20 Full crystallographic information is available from OCA.
Reference
3-Methyladenine DNA glycosylase I is an unexpected helix-hairpin-helix superfamily member., Drohat AC, Kwon K, Krosky DJ, Stivers JT, Nat Struct Biol. 2002 Sep;9(9):659-64. PMID:12161745
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