1LMZ
Solution Structure of 3-Methyladenine DNA Glycosylase I (TAG)
Summary for 1LMZ
| Entry DOI | 10.2210/pdb1lmz/pdb |
| NMR Information | BMRB: 5398 |
| Descriptor | 3-methyladenine DNA glycosylase I (TAG) (1 entity in total) |
| Functional Keywords | helix-hairpin-helix superfamily, dna glycosylase, enzyme, tag, 3-methyladenine, solution structure, nmr spectroscopy, hydrolase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 21138.13 |
| Authors | Drohat, A.C.,Kwon, K.,Krosky, D.J.,Stivers, J.T. (deposition date: 2002-05-02, release date: 2002-08-28, Last modification date: 2024-05-01) |
| Primary citation | Drohat, A.C.,Kwon, K.,Krosky, D.J.,Stivers, J.T. 3-Methyladenine DNA glycosylase I is an unexpected helix-hairpin-helix superfamily member. Nat.Struct.Biol., 9:659-664, 2002 Cited by PubMed 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. PubMed: 12161745DOI: 10.1038/nsb829 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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