5T2W

Structure of thymine DNA glycosylase bound to substrate analog 2'-F-5-formyl-dC

5T2W の概要

• エントリーDOI: 10.2210/pdb5t2w/pdb
• 分子名称: G/T mismatch-specific thymine DNA glycosylase, DNA (28-MER), DNA (27-MER), ... (4 entities in total)
• 機能のキーワード: protein-dna complex, hydrolase-dna complex, hydrolase/dna
• 由来する生物種: Homo sapiens (Human); 詳細
• 細胞内の位置: Nucleus : Q13569
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 43118.09

構造登録者

Pidugu, L.S.,Pozharski, E.,Drohat, A.C. (登録日: 2016-08-24, 公開日: 2016-11-09, 最終更新日: 2023-10-04)

主引用文献

Pidugu, L.S.,Flowers, J.W.,Coey, C.T.,Pozharski, E.,Greenberg, M.M.,Drohat, A.C.
Structural Basis for Excision of 5-Formylcytosine by Thymine DNA Glycosylase.
Biochemistry, 55:6205-6208, 2016

PubMed Abstract: Thymine DNA glycosylase (TDG) is a base excision repair enzyme with key functions in epigenetic regulation. Performing a critical step in a pathway for active DNA demethylation, TDG removes 5-formylcytosine and 5-carboxylcytosine, oxidized derivatives of 5-methylcytosine that are generated by TET (ten-eleven translocation) enzymes. We determined a crystal structure of TDG bound to DNA with a noncleavable (2'-fluoroarabino) analogue of 5-formyldeoxycytidine flipped into its active site, revealing how it recognizes and hydrolytically excises fC. Together with previous structural and biochemical findings, the results illustrate how TDG employs an adaptable active site to excise a broad variety of nucleobases from DNA.

PubMed: 27805810
DOI: 10.1021/acs.biochem.6b00982

実験手法

X-RAY DIFFRACTION (2.2 Å)