1lmz | pdb_00001lmz

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

spinqualitylabelsall models 1lmz, 25 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1lmz is a 1 chain structure with sequence from Escherichia coli (strain b). Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: TAG (Escherichia coli (strain B)) Activity: DNA-3-methyladenine glycosylase I, with EC number 3.2.2.20 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also DNA glycosylase 3D structures

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