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3.2.1.143: poly(ADP-ribose) glycohydrolase

This is an abbreviated version!
For detailed information about poly(ADP-ribose) glycohydrolase, go to the full flat file.

Word Map on EC 3.2.1.143

Reaction

(ADP-ribose)n
+
H2O
=
(ADP-ribose)n-1
 +
ADP-ribose

Synonyms

ADP-ribose glycohydrolase, ADP-ribosyl-acceptor hydrolase 3, ADPRHL2, ARH3, DrPARG, FOXG_05947, Genbank AB019366-derived protein GI 6518480, Genbank U78975-derived protein GI 2062407, glycohydrolase, poly(adenosine diphosphoribose), glycohydrolase, poly(adenosine diphosphoribose) (cattle clone 4/5), glycohydrolase, poly(adenosine diphosphoribose) (Rattus norvegicus strain BUF gene Parg), PAR glycohydrolase, PAR glyco­hydrolase, PARG, PARG1, PARG110, PARG111, PARG59, poly (ADP-ribose) glycohydrolase, poly(adenosine diphosphoribose) glycohydrolase, poly(adenosine diphosphoribose) glycosidase, poly(ADP-ribose) glycohydrolase, poly(ADP-ribose) glycohydrolase (Arabidopsis thaliana gene At2g31860), poly(ADP-ribose) glycohydrolase (Arabidopsis thaliana gene At2g31870), poly(ADP-ribose) glycohydrolase (cattly clone 4/5), poly(ADP-ribose) glycohydrolase 1, poly(ADP-ribose)glycohydrolase, poly(ADP-ribosyl) glycohydrolase, poly-ADP-glycohydrolase

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.143 poly(ADP-ribose) glycohydrolase

Crystallization

Crystallization on EC 3.2.1.143 - poly(ADP-ribose) glycohydrolase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallization of ADP-ribose bound wild-type enzyme and mutant enzymes T267K and T267R, X-ray diffraction structure determination and analysis at 1.97 A resolution, monoclinic crystals with space group P21
purified ARH3-ADPR substrate complex, sitting drop vapour diffusion method, ARH3 and ADPR are mixed in the molar ratio of 1:3, mixing of equal volumes of 11 mg/ml protein complex in 10 mM Tris-HCl, pH 8.0, and 100 mM NaCl with reservoir solution consisting of 0.1 M MES, pH 6.0, and 20% w/v PEG MME 2000, addition of 0.2 M non-detergent sulfobetaine NDSB-201, 20°C, X-ray diffraction structure determination and analysis at 1.58 A resolution, molecular replacement using the structure of apo-ARH3 (PDB ID 2FOZ) as the search model, modeling
purified enzyme in complex with ADP-ribose dimer, X-ray diffraction structure determination and analysis at 1.9 A resolution
purified recombinant full-length ARH3 wild-type enzyme and D314E mutant in complex with ADP-ribose and Mg2+, hanging drop vapor diffusion method, 10 mg/ml protein in 25 mM Tris-HCl, pH 7.5, 150 mM NaCl, 1 mM DTT, and 5% glycerol, is mixed with reservoir solution containing 22% PEG 4000, 0.1 M sodium acetate, pH 4.5, and 0.1 M MgSO4, at 22°C, crystals are briefly equilibrated in a harvesting solution containing 26% PEG 4000, 0.1 M sodium acetate, pH 4.5, 0.1 M MgSO4, and 5 mM ADP-ribose, transferred to a cryoprotectant solution (26% PEG 4000, 0.1 M sodium acetate, pH 4.5, 0.1 M MgSO4, 5 mM ADPR, and 15% glycerol), and then flash-cooled in liquid nitrogen for data collection, X-ray diffraction structure determination and analysis at 1.6-1.7 A resolution, molecular replacement using the apo-ARH3DELTAN16 structure as a search model
purified recombinant mutant K616A/Q617A/K618A/E688A/K689A/K690A, also in selenomethionine-labeld form, in complex with inhibitors, sitting drop vapour diffusion, mixing protein in SEC buffer at 7.5 mg/mL with a precipitant consisting of 28% PEG 3350, 0.2 M magnesium chloride, 0.1 M PCTP (0.04 M sodium propionate, 0.02 M sodium cacodylate, 0.04 M Bis-Tris propane), pH 7.5, in a 1:1 ratio to give a 0.004 ml drop, 20°C, X-ray diffraction structure determination and analysis at 1.75-1.83 A resolution, molecular replacement
enzyme catalytic domain free or in complexes with ADP-ribose and inhibitor ADP-HPD, as well as four enzyme catalytic residues mutants, X-ray diffraction structure determination and analysis
purified truncated native and selenomethionine-labeled enzymes comprising residues 385-972 and lacking the A-domain, free or in complex with adenosine diphosphate (hydroxymethyl) pyrrolidinediol, hanging drop vapour diffusion method, mixing of 15 mg/ml protein in 25 mM HEPES, pH 7.5, 150 mM NaCl, 5% glycerol and 2 mM DTT, with an equal volume of well solution containing 16-20% w/v PEG 2000 monomethylether, 0.1 M Tris-HCl, pH 7.5, 0.1 M NaCl, and 0.2 M potassium thiocyanate, 22°C, X-ray diffraction structure determination and analysis at 1.95 A resolution
purified recombinant His-tagged enzyme in complex with ADP-ribose or inhibitor RBPI-3, and as selenomethionine-labeled enzyme, sitting drop vapour diffusion method, 15 mg/ml protein is mixed with a 1:1 molar ratio with ADP-ribose, and with an equal volume of a solution containing 0.15 M potassium thiocyanate, 0.1 M Tris, pH 8.5, and 15% PEG 6000, or with 0.2 M potassium bromide, 0.1 M Tris, pH 7.5, and 15% PEG 4000, X-ray diffraction structure determination and analysis at 1.95 A resolution
in complexes with ADP-ribose and inhibitor adenosine 5'-diphosphate (hydroxymethyl) pyrrolidinediol
-
reaction mechanism modelling on crystal structure PDB ID 3SIG