3BIE
X-ray structure of E coli AlkB bound to dsDNA containing 1meA/T with Mn and 2KG
3BIE の概要
エントリーDOI | 10.2210/pdb3bie/pdb |
関連するPDBエントリー | 2FD8 2IUW 2QXQ |
分子名称 | Alpha-ketoglutarate-dependent dioxygenase alkB, DNA (5'-D(P*DAP*DGP*DGP*DTP*DAP*DAP*(MA7)P*DAP*DCP*DCP*DGP*DT)-3'), DNA (5'-D(*DAP*DAP*DCP*DGP*DGP*DTP*DTP*DTP*DTP*DAP*DCP*DCP*DT)-3'), ... (6 entities in total) |
機能のキーワード | dioxygenase, protein dna interaction, cross-linking, alkylation repair, oxidoreductase-dna complex, oxidoreductase/dna |
由来する生物種 | Escherichia coli K12 |
タンパク質・核酸の鎖数 | 3 |
化学式量合計 | 30356.90 |
構造登録者 | |
主引用文献 | Yang, C.-G.,Yi, C.,Duguid, E.M.,Sullivan, C.T.,Jian, X.,Rice, P.A.,He, C. Crystal structures of DNA/RNA repair enzymes AlkB and ABH2 bound to dsDNA Nature, 452:961-965, 2008 Cited by PubMed Abstract: Escherichia coli AlkB and its human homologues ABH2 and ABH3 repair DNA/RNA base lesions by using a direct oxidative dealkylation mechanism. ABH2 has the primary role of guarding mammalian genomes against 1-meA damage by repairing this lesion in double-stranded DNA (dsDNA), whereas AlkB and ABH3 preferentially repair single-stranded DNA (ssDNA) lesions and can repair damaged bases in RNA. Here we show the first crystal structures of AlkB-dsDNA and ABH2-dsDNA complexes, stabilized by a chemical cross-linking strategy. This study reveals that AlkB uses an unprecedented base-flipping mechanism to access the damaged base: it squeezes together the two bases flanking the flipped-out one to maintain the base stack, explaining the preference of AlkB for repairing ssDNA lesions over dsDNA ones. In addition, the first crystal structure of ABH2, presented here, provides a structural basis for designing inhibitors of this human DNA repair protein. PubMed: 18432238DOI: 10.1038/nature06889 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.68 Å) |
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