PMID:12161745

Citation	Drohat, AC, Kwon, K, Krosky, DJ and Stivers, JT (2002) 3-Methyladenine DNA glycosylase I is an unexpected helix-hairpin-helix superfamily member. Nat. Struct. Biol. 9:659-64
Abstract	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.
Links	PubMed Online version:10.1038/nsb829
Keywords	Amino Acid Sequence; DNA Glycosylases; Models, Molecular; Molecular Sequence Data; N-Glycosyl Hydrolases/chemistry; Nuclear Magnetic Resonance, Biomolecular; Protein Conformation; Sequence Homology, Amino Acid; Spectrometry, Fluorescence
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