Structural highlights
Function
[3MG1_ECOLI] Hydrolysis of the deoxyribose N-glycosidic bond to excise 3-methyladenine from the damaged DNA polymer formed by alkylation lesions.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Drohat AC, Kwon K, Krosky DJ, Stivers JT. 3-Methyladenine DNA glycosylase I is an unexpected helix-hairpin-helix superfamily member. Nat Struct Biol. 2002 Sep;9(9):659-64. PMID:12161745 doi:10.1038/nsb829
