3UO7

Crystal structure of Human Thymine DNA Glycosylase Bound to Substrate 5-carboxylcytosine

3UO7 の概要

• エントリーDOI: 10.2210/pdb3uo7/pdb
• 関連するPDBエントリー: 3UOB
• 分子名称: 5'-D(*CP*AP*GP*CP*TP*CP*TP*GP*TP*AP*CP*AP*TP*GP*AP*GP*CP*AP*GP*TP*GP*GP*A)-3', 5'-D(*CP*CP*AP*CP*TP*GP*CP*TP*CP*AP*(1CC)P*GP*TP*AP*CP*AP*GP*AP*GP*CP*TP*GP*T)-3', G/T mismatch-specific thymine DNA glycosylase (3 entities in total)
• 機能のキーワード: dsdna with 5cac, hydrolase-dna complex, hydrolase/dna
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus : Q13569
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 59607.68

構造登録者

Zhang, L.,He, C. (登録日: 2011-11-16, 公開日: 2012-02-15, 最終更新日: 2023-09-13)

主引用文献

Zhang, L.,Lu, X.,Lu, J.,Liang, H.,Dai, Q.,Xu, G.L.,Luo, C.,Jiang, H.,He, C.
Thymine DNA glycosylase specifically recognizes 5-carboxylcytosine-modified DNA.
Nat.Chem.Biol., 8:328-330, 2012

PubMed Abstract: Human thymine DNA glycosylase (hTDG) efficiently excises 5-carboxylcytosine (5caC), a key oxidation product of 5-methylcytosine in genomic DNA, in a recently discovered cytosine demethylation pathway. We present here the crystal structures of the hTDG catalytic domain in complex with duplex DNA containing either 5caC or a fluorinated analog. These structures, together with biochemical and computational analyses, reveal that 5caC is specifically recognized in the active site of hTDG, supporting the role of TDG in mammalian 5-methylcytosine demethylation.

PubMed: 22327402
DOI: 10.1038/nchembio.914

実験手法

X-RAY DIFFRACTION (3.002 Å)