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1lmz
From Proteopedia
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| Gene: | TAG (Escherichia coli) | ||||||
| Activity: | DNA-3-methyladenine glycosylase I, with EC number 3.2.2.20 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
Page seeded by OCA on Sun Mar 30 22:04:44 2008
