5ITR

Crystal Structure of Human NEIL1(P2G) bound to duplex DNA containing THF

5ITR の概要

• エントリーDOI: 10.2210/pdb5itr/pdb
• 関連するPDBエントリー: 5ITQ 5ITT 5ITU 5ITX 5ITY
• 分子名称: Endonuclease 8-like 1, DNA (26-MER), ... (4 entities in total)
• 機能のキーワード: dna glycosylase neil1 fpg nei base excision repair, dna binding protein-dna complex, dna binding protein/dna
• 由来する生物種: Homo sapiens (Human); 詳細
• 細胞内の位置: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome : Q96FI4
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 158639.47

構造登録者

Zhu, C.,Lu, L.,Zhang, J.,Yue, Z.,Song, J.,Zong, S.,Liu, M.,Stovicek, O.,Gao, Y.,Yi, C. (登録日: 2016-03-17, 公開日: 2016-07-06, 最終更新日: 2023-11-08)

主引用文献

Zhu, C.,Lu, L.,Zhang, J.,Yue, Z.,Song, J.,Zong, S.,Liu, M.,Stovicek, O.,Gao, Y.Q.,Yi, C.
Tautomerization-dependent recognition and excision of oxidation damage in base-excision DNA repair
Proc.Natl.Acad.Sci.USA, 113:7792-7797, 2016

PubMed Abstract: NEIL1 (Nei-like 1) is a DNA repair glycosylase guarding the mammalian genome against oxidized DNA bases. As the first enzymes in the base-excision repair pathway, glycosylases must recognize the cognate substrates and catalyze their excision. Here we present crystal structures of human NEIL1 bound to a range of duplex DNA. Together with computational and biochemical analyses, our results suggest that NEIL1 promotes tautomerization of thymine glycol (Tg)-a preferred substrate-for optimal binding in its active site. Moreover, this tautomerization event also facilitates NEIL1-catalyzed Tg excision. To our knowledge, the present example represents the first documented case of enzyme-promoted tautomerization for efficient substrate recognition and catalysis in an enzyme-catalyzed reaction.

PubMed: 27354518
DOI: 10.1073/pnas.1604591113

実験手法

X-RAY DIFFRACTION (2.46 Å)