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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DOI10.2210/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
Yi, C.,Yang, C.-G. (登録日: 2007-11-30, 公開日: 2008-04-22, 最終更新日: 2024-10-16)
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: 18432238
DOI: 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)
構造検証レポート
Validation report summary of 3bie
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-05-14に公開中

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