2jhj | pdb_00002jhj

3-methyladenine dna-glycosylase from Archaeoglobus fulgidus

spinqualitylabelsall models 2jhj, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2jhj is a 2 chain structure with sequence from Arcfl. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL, NA Related: 2jhn Activity: DNA-3-methyladenine glycosylase II, with EC number 3.2.2.21 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 N(1)-methyladenine (m(1)A) and N(3)-methylcytosine (m(3)C) are major toxic and mutagenic lesions induced by alkylation in single-stranded DNA. In bacteria and mammals, m(1)A and m(3)C were recently shown to be repaired by AlkB-mediated oxidative demethylation, a direct DNA damage reversal mechanism. No AlkB gene homologues have been identified in Archaea. We report that m(1)A and m(3)C are repaired by the AfAlkA base excision repair glycosylase of Archaeoglobus fulgidus, suggesting a different repair mechanism for these lesions in the third domain of life. In addition, AfAlkA was found to effect a robust excision of 1,N(6)-ethenoadenine. We present a high-resolution crystal structure of AfAlkA, which, together with the characterization of several site-directed mutants, forms a molecular rationalization for the newly discovered base excision activity. Structural basis for enzymatic excision of N1-methyladenine and N3-methylcytosine from DNA.,Leiros I, Nabong MP, Grosvik K, Ringvoll J, Haugland GT, Uldal L, Reite K, Olsbu IK, Knaevelsrud I, Moe E, Andersen OA, Birkeland NK, Ruoff P, Klungland A, Bjelland S EMBO J. 2007 Apr 18;26(8):2206-17. Epub 2007 Mar 29. PMID:17396151 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also DNA glycosylase

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