2D07

Crystal Structure of SUMO-3-modified Thymine-DNA Glycosylase

2D07 の概要

• エントリーDOI: 10.2210/pdb2d07/pdb
• 分子名称: G/T mismatch-specific thymine DNA glycosylase, Ubiquitin-like protein SMT3B (3 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 P61956
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 36800.96

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: 2005-07-26, 公開日: 2006-06-06, 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 SUMO-3-modified Thymine-DNA Glycosylase
J.Mol.Biol., 359:137-147, 2006

PubMed Abstract: Modification of cellular proteins by the small ubiquitin-like modifier SUMO is important in regulating various cellular events. Many different nuclear proteins are targeted by SUMO, and the functional consequences of this modification are diverse. For most proteins, however, the functional and structural consequences of modification by specific SUMO isomers are unclear. Conjugation of SUMO to thymine-DNA glycosylase (TDG) induces the dissociation of TDG from its product DNA. Structure determination of the TDG central region conjugated to SUMO-1 previously suggested a mechanism in which the SUMOylation-induced conformational change in the C-terminal region of TDG releases TDG from tight binding to its product DNA. Here, we have determined the crystal structure of the central region of TDG conjugated to SUMO-3. The overall structure of SUMO-3-conjugated TDG is similar to the previously reported structure of TDG conjugated to SUMO-1, despite the relatively low level of amino acid sequence similarity between SUMO-3 and SUMO-1. The two structures revealed that the sequence of TDG that resembles the SUMO-binding motif (SBM) can form an intermolecular beta-sheet with either SUMO-1 or SUMO-3. Structural comparison with the canonical SBM shows that this SBM-like sequence of TDG retains all of the characteristic interactions of the SBM, indicating sequence diversity in the SBM.

PubMed: 16626738
DOI: 10.1016/j.jmb.2006.03.036

実験手法

X-RAY DIFFRACTION (2.1 Å)