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5ZDE

Crystal structure of poly(ADP-ribose) glycohydrolase (PARG) from Deinococcus radiodurans in complex with ADP-ribose (P3221)

Summary for 5ZDE
Entry DOI10.2210/pdb5zde/pdb
DescriptorPoly ADP-ribose glycohydrolase, [(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]METHYL[HYDROXY-[[(2R,3S,4R,5S)-3,4,5-TRIHYDROXYOXOLAN-2-YL]METHOXY]PHOSPHORYL] HYDROGEN PHOSPHATE (2 entities in total)
Functional Keywordsadp-ribose, poly(adp-ribose) glycohydrolase, hydrolase
Biological sourceDeinococcus radiodurans R1
Total number of polymer chains1
Total formula weight27949.21
Authors
Cho, C.C.,Hsu, C.H. (deposition date: 2018-02-23, release date: 2019-02-27, Last modification date: 2025-04-09)
Primary citationCho, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.8 Å)
Structure validation

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