3UEK

Crystal structure of the catalytic domain of rat poly (ADP-ribose) glycohydrolase

3UEK の概要

• エントリーDOI: 10.2210/pdb3uek/pdb
• 関連するPDBエントリー: 3UEL
• 分子名称: Poly(ADP-ribose) glycohydrolase (2 entities in total)
• 機能のキーワード: mammalian parg, macrodomain, hydrolase
• 由来する生物種: Rattus norvegicus (brown rat,rat,rats)
• 細胞内の位置: Nucleus (By similarity): Q9QYM2
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 67780.16

構造登録者

Kim, I.K.,Kiefer, J.R.,Stegemann, R.A.,Classen, S.,Tainer, J.A.,Ellenberger, T. (登録日: 2011-10-30, 公開日: 2012-05-23, 最終更新日: 2024-02-28)

主引用文献

Kim, I.K.,Kiefer, J.R.,Ho, C.M.,Stegeman, R.A.,Classen, S.,Tainer, J.A.,Ellenberger, T.
Structure of mammalian poly(ADP-ribose) glycohydrolase reveals a flexible tyrosine clasp as a substrate-binding element.
Nat.Struct.Mol.Biol., 19:653-656, 2012

PubMed Abstract: Reversible post-translational modification by poly(ADP-ribose) (PAR) regulates chromatin structure, DNA repair and cell fate in response to genotoxic stress. PAR glycohydrolase (PARG) removes PAR chains from poly ADP-ribosylated proteins to restore protein function and release oligo(ADP-ribose) chains to signal damage. Here we report crystal structures of mammalian PARG and its complex with a substrate mimic that reveal an open substrate-binding site and a unique 'tyrosine clasp' enabling endoglycosidic cleavage of branched PAR chains.

PubMed: 22609859
DOI: 10.1038/nsmb.2305

実験手法

X-RAY DIFFRACTION (1.95 Å)