This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1lmz
From Proteopedia
|
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
Page seeded by OCA on Tue Nov 20 20:41:16 2007
