5ZDA

Crystal structure of poly(ADP-ribose) glycohydrolase (PARG) from Deinococcus radiodurans in apo form

5ZDA の概要

• エントリーDOI: 10.2210/pdb5zda/pdb
• 分子名称: poly ADP-ribose glycohydrolase, SULFATE ION (3 entities in total)
• 機能のキーワード: adp-ribose, poly(adp-ribose) glycohydrolase, hydrolase
• 由来する生物種: Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 27850.40

構造登録者

Cho, C.C.,Hsu, C.H. (登録日: 2018-02-23, 公開日: 2019-02-27, 最終更新日: 2023-11-22)

主引用文献

Cho, C.C.,Chien, C.Y.,Chiu, Y.C.,Lin, M.H.,Hsu, C.H.
Structural and biochemical evidence supporting poly ADP-ribosylation in the bacterium Deinococcus radiodurans.
Nat Commun, 10:1491-1491, 2019

PubMed Abstract: Poly-ADP-ribosylation, a post-translational modification involved in various cellular processes, is well characterized in eukaryotes but thought to be devoid in bacteria. Here, we solve crystal structures of ADP-ribose-bound poly(ADP-ribose)glycohydrolase from the radioresistant bacterium Deinococcus radiodurans (DrPARG), revealing a solvent-accessible 2'-hydroxy group of ADP-ribose, which suggests that DrPARG may possess endo-glycohydrolase activity toward poly-ADP-ribose (PAR). We confirm the existence of PAR in D. radiodurans and show that disruption of DrPARG expression causes accumulation of endogenous PAR and compromises recovery from UV radiation damage. Moreover, endogenous PAR levels in D. radiodurans are elevated after UV irradiation, indicating that PARylation may be involved in resistance to genotoxic stresses. These findings provide structural insights into a bacterial-type PARG and suggest the existence of a prokaryotic PARylation machinery that may be involved in stress responses.

PubMed: 30940816
DOI: 10.1038/s41467-019-09153-6

実験手法

X-RAY DIFFRACTION (1.548 Å)