1WYW

Crystal Structure of SUMO1-conjugated thymine DNA glycosylase

1WYW の概要

• エントリーDOI: 10.2210/pdb1wyw/pdb
• 分子名称: G/T mismatch-specific thymine DNA glycosylase, Ubiquitin-like protein SMT3C, CHLORIDE ION, ... (6 entities in total)
• 機能のキーワード: hydrolase
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Nucleus: Q13569; Nucleus membrane: P63165
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 37577.47

構造登録者

Baba, D.,Maita, N.,Jee, J.G.,Uchimura, Y.,Saitoh, H.,Sugasawa, K.,Hanaoka, F.,Tochio, H.,Hiroaki, H.,Shirakawa, M. (登録日: 2005-02-17, 公開日: 2005-06-21, 最終更新日: 2023-10-25)

主引用文献

Baba, D.,Maita, N.,Jee, J.G.,Uchimura, Y.,Saitoh, H.,Sugasawa, K.,Hanaoka, F.,Tochio, H.,Hiroaki, H.,Shirakawa, M.
Crystal structure of thymine DNA glycosylase conjugated to SUMO-1.
Nature, 435:979-982, 2005

PubMed Abstract: Members of the small ubiquitin-like modifier (SUMO) family can be covalently attached to the lysine residue of a target protein through an enzymatic pathway similar to that used in ubiquitin conjugation, and are involved in various cellular events that do not rely on degradative signalling via the proteasome or lysosome. However, little is known about the molecular mechanisms of SUMO-modification-induced protein functional transfer. During DNA mismatch repair, SUMO conjugation of the uracil/thymine DNA glycosylase TDG promotes the release of TDG from the abasic (AP) site created after base excision, and coordinates its transfer to AP endonuclease 1, which catalyses the next step in the repair pathway. Here we report the crystal structure of the central region of human TDG conjugated to SUMO-1 at 2.1 A resolution. The structure reveals a helix protruding from the protein surface, which presumably interferes with the product DNA and thus promotes the dissociation of TDG from the DNA molecule. This helix is formed by covalent and non-covalent contacts between TDG and SUMO-1. The non-covalent contacts are also essential for release from the product DNA, as verified by mutagenesis.

PubMed: 15959518
DOI: 10.1038/nature03634

実験手法

X-RAY DIFFRACTION (2.1 Å)