5ZDB
Crystal structure of poly(ADP-ribose) glycohydrolase (PARG) from Deinococcus radiodurans in complex with ADP-ribose (P21)
Summary for 5ZDB
| Entry DOI | 10.2210/pdb5zdb/pdb |
| Descriptor | Poly 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 (3 entities in total) |
| Functional Keywords | adp-ribose, poly(adp-ribose) glycohydrolase, hydrolase |
| Biological source | Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422) |
| Total number of polymer chains | 2 |
| Total formula weight | 56318.98 |
| Authors | |
| Primary citation | 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 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: 30940816DOI: 10.1038/s41467-019-09153-6 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.972 Å) |
Structure validation
Download full validation report
