4B22

Unprecedented sculpting of DNA at abasic sites by DNA glycosylase homolog Mag2

4B22 の概要

• エントリーDOI: 10.2210/pdb4b22/pdb
• 関連するPDBエントリー: 4B21 4B23 4B24
• 分子名称: MAG2, DNA-3-METHYLADENINE GLYCOSYLASE 2, 5'-D(*GP*CP*TP*AP*CP*(3DR)P*CP*AP*TP*CP*GP)-3', 5'-D(*CP*GP*AP*TP*GP*GP*GP*TP*AP*GP*CP)-3', ... (4 entities in total)
• 機能のキーワード: hydrolase, helix-hairpin-helix dna glycosylase homologue
• 由来する生物種: SCHIZOSACCHAROMYCES POMBE; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 32961.42

構造登録者

Dalhus, B.,Nilsen, L.,Korvald, H.,Huffman, J.,Forstrom, R.J.,McMurray, C.T.,Alseth, I.,Tainer, J.A.,Bjoras, M. (登録日: 2012-07-12, 公開日: 2013-01-09, 最終更新日: 2024-05-08)

主引用文献

Dalhus, B.,Nilsen, L.,Korvald, H.,Huffman, J.,Forstrom, R.J.,Mcmurray, C.T.,Alseth, I.,Tainer, J.A.,Bjoras, M.
Sculpting of DNA at Abasic Sites by DNA Glycosylase Homolog Mag2.
Structure, 21:154-, 2013

PubMed Abstract: Modifications and loss of bases are frequent types of DNA lesions, often handled by the base excision repair (BER) pathway. BER is initiated by DNA glycosylases, generating abasic (AP) sites that are subsequently cleaved by AP endonucleases, which further pass on nicked DNA to downstream DNA polymerases and ligases. The coordinated handover of cytotoxic intermediates between different BER enzymes is most likely facilitated by the DNA conformation. Here, we present the atomic structure of Schizosaccharomyces pombe Mag2 in complex with DNA to reveal an unexpected structural basis for nonenzymatic AP site recognition with an unflipped AP site. Two surface-exposed loops intercalate and widen the DNA minor groove to generate a DNA conformation previously only found in the mismatch repair MutS-DNA complex. Consequently, the molecular role of Mag2 appears to be AP site recognition and protection, while possibly facilitating damage signaling by structurally sculpting the DNA substrate.

PubMed: 23245849
DOI: 10.1016/J.STR.2012.11.004

実験手法

X-RAY DIFFRACTION (1.9 Å)