4EPP

Canonical poly(ADP-ribose) glycohydrolase from Tetrahymena thermophila.

4EPP の概要

• エントリーDOI: 10.2210/pdb4epp/pdb
• 関連するPDBエントリー: 4EPQ
• 分子名称: Poly(ADP-ribose) glycohydrolase, ADENOSINE-5-DIPHOSPHORIBOSE (3 entities in total)
• 機能のキーワード: marco domain, par, hydrolase
• 由来する生物種: Tetrahymena thermophila
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 112890.69

構造登録者

Dunstan, M.S.,Leys, D. (登録日: 2012-04-17, 公開日: 2012-06-20, 最終更新日: 2024-02-28)

主引用文献

Dunstan, M.S.,Barkauskaite, E.,Lafite, P.,Knezevic, C.E.,Brassington, A.,Ahel, M.,Hergenrother, P.J.,Leys, D.,Ahel, I.
Structure and mechanism of a canonical poly(ADP-ribose) glycohydrolase.
Nat Commun, 3:878-878, 2012

PubMed Abstract: Poly(ADP-ribosyl)ation is a reversible post-translational protein modification involved in the regulation of a number of cellular processes including DNA repair, chromatin structure, mitosis, transcription, checkpoint activation, apoptosis and asexual development. The reversion of poly(ADP-ribosyl)ation is catalysed by poly(ADP-ribose) (PAR) glycohydrolase (PARG), which specifically targets the unique PAR (1''-2') ribose-ribose bonds. Here we report the structure and mechanism of the first canonical PARG from the protozoan Tetrahymena thermophila. In addition, we reveal the structure of T. thermophila PARG in a complex with a novel rhodanine-containing mammalian PARG inhibitor RBPI-3. Our data demonstrate that the protozoan PARG represents a good model for human PARG and is therefore likely to prove useful in guiding structure-based discovery of new classes of PARG inhibitors.

PubMed: 22673905
DOI: 10.1038/ncomms1889

実験手法

X-RAY DIFFRACTION (1.95 Å)