4NA5

Crystal structure of mouse poly(ADP-ribose) glycohydrolase (PARG) catalytic domain mutant E748N

4NA5 の概要

• エントリーDOI: 10.2210/pdb4na5/pdb
• 関連するPDBエントリー: 4FC2 4N9Y 4N9Z 4NA0 4NA4
• 分子名称: Poly(ADP-ribose) glycohydrolase, SULFATE ION (3 entities in total)
• 機能のキーワード: poly(adp-ribose) glycohydrolase, hydrolase
• 由来する生物種: Mus musculus (mouse)
• 細胞内の位置: Nucleus (By similarity): O88622
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 60516.83

構造登録者

Wang, Z.,Cheng, Z.,Xu, W. (登録日: 2013-10-21, 公開日: 2014-01-29, 最終更新日: 2024-02-28)

主引用文献

Wang, Z.,Gagne, J.P.,Poirier, G.G.,Xu, W.
Crystallographic and biochemical analysis of the mouse poly(ADP-ribose) glycohydrolase.
Plos One, 9:e86010-e86010, 2014

PubMed Abstract: Protein poly(ADP-ribosyl)ation (PARylation) regulates a number of important cellular processes. Poly(ADP-ribose) glycohydrolase (PARG) is the primary enzyme responsible for hydrolyzing the poly(ADP-ribose) (PAR) polymer in vivo. Here we report crystal structures of the mouse PARG (mPARG) catalytic domain, its complexes with ADP-ribose (ADPr) and a PARG inhibitor ADP-HPD, as well as four PARG catalytic residues mutants. With these structures and biochemical analysis of 20 mPARG mutants, we provide a structural basis for understanding how the PAR polymer is recognized and hydrolyzed by mPARG. The structures and activity complementation experiment also suggest how the N-terminal flexible peptide preceding the PARG catalytic domain may regulate the enzymatic activity of PARG. This study contributes to our understanding of PARG catalytic and regulatory mechanisms as well as the rational design of PARG inhibitors.

PubMed: 24465839
DOI: 10.1371/journal.pone.0086010

実験手法

X-RAY DIFFRACTION (2 Å)