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5.3.1.6: ribose-5-phosphate isomerase

This is an abbreviated version!
For detailed information about ribose-5-phosphate isomerase, go to the full flat file.

Word Map on EC 5.3.1.6

Reaction

D-ribose 5-phosphate
=
D-ribulose 5-phosphate

Synonyms

5-phosphate ketol-isomerase, 5-Phosphoribose isomerase, CTRPI, CTRpiB, D-Ribose 5-phosphate isomerase, D-ribose-5-phosphate isomerase, D-ribose-5-phosphate isomerase A, D-ribose-5-phosphate isomerase B, D-ribose-5-phosphate ketol-isomerase, D-xylose ketol-isomerase, EcRpiB, Isomerase, ribose phosphate, LINJ_28_2100, LMJF_28_1970, MJ1603, MtRpiB, Phosphopentoisomerase, Phosphopentose isomerase, Phosphoriboisomerase, ribose 5-phosphate isomerase A, Ribose phosphate isomerase, Ribose-5-P isomerase, ribose-5-phosphate isomerase, ribose-5-phosphate isomerase B, ribose-5-phosphate isomerase type B, Ribosephosphate isomerase A, Ribosephosphate isomerase B, RPI, RPI2 protein, RpiA, RpiB, SMU1234, SMU2142, Tc00.1047053509199.24, TM1080, type B ribose 5-phosphate isomerase, type B ribose-5-phosphate isomerase, type B Rpi

ECTree

     5 Isomerases
         5.3 Intramolecular oxidoreductases
             5.3.1 Interconverting aldoses and ketoses, and related compounds
                5.3.1.6 ribose-5-phosphate isomerase

Crystallization

Crystallization on EC 5.3.1.6 - ribose-5-phosphate isomerase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with ribose 5-phosphate, ribose or allose, sitting drop vapor diffusion method, using 0.05 M Tris pH 7.0, 10% (w/v) PEG 8000, 0.15 M magnesium chloride, and 0.2 M potassium chloride
purified recombinant RpiB, sitting drop vapour diffusion method, 0.001 ml of 7 mg/ml protein in mM Tris-HCl buffer pH 7.5 is mixed with 0.001 ml of reservoir solution, containing 0.05 M Tris, pH 7.0, 10% PEG 8000, 0.15 M MgCl2 and 0.2 M KCl, and equilibrated against 1 ml of reservoir solution, 3 weeks, flash-cooling in liquid nitrogen with a cryoprotectant solution containing 65 mM Tris pH 7.0, 13% PEG 8000, 195 mM MgCl2, 260 mM KCl and 20% glycerol, X-ray diffraction structure determination and analysis at 1.9 A resolution, modeling
-
molecular dockng using L-xylose and D-ribose as the substrate. Residue M95 seems to be a determinant residue for the specificity on free sugars
-
co-crystallization in the presence of 20 mM ribose-5-phosphate or 20 mM ribose-5-phosphate with 12 mM MnCl2, sitting drop vapor diffusion method, using 0.1 M Na citrate pH 5.0, 20% (w/v) PEG 6000
hanging drop vapor diffusion method, enzyme form RpiA
-
hanging drop vapor diffusion method, structure of a complex with arabinose 5-phosphate at 1.25 A resolution
comparison of structures and active sites of RpiB from Leishmania major and RpiA and docking of substrate. Both enzymes form a homomultimer, which in the enzymes of type B is essential to form the active site. Distinct residue types participate in the catalytic reaction in the two enzymes
homology modeling of wild type and mutants
comparison of structures and active sites of RpiB and RpiA from Homo sapiens (HsRpiA). Both enzymes form a homomultimer, which in the enzymes of type B is essential to form the active site. Distinct residue types participate in the catalytic reaction in the two enzymes. In LmRpiB, residues Y46,H11, H102 and H138 are part of the active site
purified recombinant MJ1603, microbatch-under-oil method, 0.0005 ml of 8.1 mg/ml protein in 20 mM Tris-HCl buffer, pH 8.0, containing 200 mM NaCl are mixed with 0.0005 ml of crystallization reagent, consisting of 0.1 M acetate, pH 4.5 containing 40% v/v 1,2-propanediol and 0.05 M calcium acetate, 18°C. The mixture is covered with 0.015 ml silicone and paraffin oil, X-ray diffraction structure determination and analysis at 1.78 A resolution, molecular replacement and modeling
hanging drop vapour diffusion method, X-ray structure of ribose-5-phosphate isomerase B in complex with the inhibitors 4-phosphono-D-erythronohydroxamate and 4-phospho-D-erythronate refined to resolutions of 2.1 and 2.2 A
in complex with 5-deoxy-5-phospho-D-ribonohydroxamate, hanging drop vapour diffusion method, with 15% PEG 8000, 0.1 M MES buffer, pH 6, 5% PEG 1000, and 0.2 M Li2SO4, or in complex with D-ribose 5-phosphate, sitting drop vapour diffusion method, with 20% PEG 3K, 0.1 M Tris, pH 7, and 0.2 M Ca acetate
sitting drop vapour diffusion method
-
molecular replacement at 2.9 A resolution
-
hanging drop vapor diffusion method, crystal structure of the free enzyme and the complex with D-4-phosphoerythronic acid
2.1 A resolution crystal structure. Crystals are cryo-protected by transfering through crystallization solution with progressively higher ethylene glycol concentration up to 30% v/v and then flash cooled in liquid nitrogen. The protein crystallizes in space group F432 with cell dimensions a = b = c = 209A, corresponding to one molecule per asymmetric unit and a solvent content of 47%
-
sitting drop vapor diffusion method, using 20% (w/v) PEG 3350, 0.2 M ammonium acetate, 0.1 M HEPES pH 7.5, 0.1 M NaCl, 2.0 M ammonium sulfate
sitting drop vapor diffusion method, using 20% (w/v) PEG 3350, 0.2 M ammonium acetate, 0.1 M Tris-HCl pH 8.5 and 25% (w/v) PEG 3350, 0.2 M MgCl2, 0.1 M Tris-HCl pH 8.5
the structure of the enzyme is determined to 1.90 A resolution by multiwavelength anomalous diffraction phasing from a SeMet labeled protein
crystal structure of enzyme complexed with the open chain form of the ribose 5-phosphate and the open chain form of the C2 epimeric inhibitor arabinose 5-phosphate as well as the apo form at high resolution
-
RpiB (wild type or C69A mutant enzyme), sitting drop vapor diffusion method, using 0.5% (v/v) Jeffamine ED-2001, 0.1 M HEPES, 1.1 M Na-malonate (pH 7.0) for the wild type enzyme in complex with phosphate, or 0.8 M Na?K phosphate (pH 8.2) for the mutant enzyme C69A in complex with phosphate, or 20% (w/v) poly(ethyleneglycol) 550 monomethyl ether, 0.1 M NaCl, 0.1 M bicine (pH 9.0) for the wild type enzyme in complex with D-ribose 5-phosphate, or 20% (w/v) poly(ethylene glycol) 6000, 0.2 M ammonium chloride, 0.1 M Tris-HCl (pH 8.0) for wild type enzyme in complex with 4-phospho-D-erythronohydroxamic acid, or 20% (w/v) poly(ethylene glycol) 3350, 0.2 M sodium acetate, 0.1 M bis-Tris propane (pH 8.5) for mutant enzyme C69A in complex with allose 6-phosphate
open form RpiA in complex with substrate ribose 5-phosphate, the closed form complexed with arabinose-5-phosphate, and the apo-RpiA, hanging drop vapor diffusion method, 0.002 ml of 30 mg/ml protein in 20 mM HEPES, pH 7.5, and 150 mM KCl are mixed with 0.002 ml of a reservoir solution containing 50 mM succinate, pH 4.1, 180 mM ammonium sulfate, and 8% PEG 4000, 3 days, 20°C, for complexed enzyme addition of 20 mM ligand, X-ray diffraction structure determination and analysis at 1.49-2.07 A resolution, molecular replacement