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2JHN

3-methyladenine dna-glycosylase from Archaeoglobus fulgidus

Summary for 2JHN
Entry DOI10.2210/pdb2jhn/pdb
Related2JHJ
Descriptor3-METHYLADENINE DNA-GLYCOSYLASE, MERCURIBENZOIC ACID, MERCURY (II) ION, ... (7 entities in total)
Functional Keywordsalka, dna repair, n1-methyladenine, n3-methylcytosine, hyperthermophiles, archaeoglobus fulgidus, hydrolase
Biological sourceARCHAEOGLOBUS FULGIDUS
Total number of polymer chains2
Total formula weight70848.91
Authors
Primary citationLeiros, I.,Nabong, M.P.,Grosvik, K.,Ringvoll, J.,Haugland, G.T.,Uldal, L.,Reite, K.,Olsbu, I.K.,Knaevelsrud, I.,Moe, E.,Andersen, O.A.,Birkeland, N.K.,Ruoff, P.,Klungland, A.,Bjelland, S.
Structural Basis for Enzymatic Excision of N1-Methyladenine and N3-Methylcytosine from DNA
Embo J., 26:2206-, 2007
Cited by
PubMed Abstract: 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.
PubMed: 17396151
DOI: 10.1038/SJ.EMBOJ.7601662
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

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