1LMZ: Solution Structure of 3-Methyladenine DNA Glycosylase I (TAG)

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.
PDB ID: 1LMZDownload
MMDB ID: 20460
PDB Deposition Date: 2002/5/2
Updated in MMDB: 2007/11
Experimental Method:
solution nmr
Source Organism:
Similar Structures:
Biological Unit for 1LMZ: monomeric; determined by author
Molecular Components in 1LMZ
Label Count Molecule
Protein (1 molecule)
3-methyladenine DNA Glycosylase I (Tag)(Gene symbol: tag)
Molecule annotation
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