2.4.2.2: pyrimidine-nucleoside phosphorylase
This is an abbreviated version!
For detailed information about pyrimidine-nucleoside phosphorylase, go to the full flat file.
Word Map on EC 2.4.2.2
Reaction
Synonyms
AmPyNP, BbPyNP, BfPyNP, BsPyNP, deoA, EC 2.4.2.23, GsPyNP, GtPyNP, LpPyNP, nucleoside phosphorylase, PDP, phosphorylase, pyrimidine nucleoside, Py-NPase, PYNP, pynpase, pyrimidine nucleoside phosphorylase, pyrimidine ribonucleoside phosphorylase, pyrimidine-nucleoside phosphorylase, pyrimidine/purine nucleoside phosphorylase, TTHA1771, TtPyNP, udp, UPase
ECTree
2.4.2.2 pyrimidine-nucleoside phosphorylaseAdvanced search results
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results (Crystallization
Crystallization on EC 2.4.2.2 - pyrimidine-nucleoside phosphorylase
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CRYSTALLIZATION (Commentary) 
ORGANISM
UNIPROT
LITERATURE
purified enzyme in complex with imidazole and sulfate, sitting drop vapour diffusion, mixing of 0.002 ml of 16 mg/ml protein in 20 mM Tris-HCl, 500 mM KCl with 0.002 ml of reservoir solution containing 0.2 M ammonium acetate, 0.1 M bis-Tris, pH 5.5, X-ray diffraction structure determination and analysis at 1.88 A resolution
crystal structure of the enzyme with the substrate analog, pseudouridine, in its active site is solved to 2.1 A
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hanging-drop vapor diffusion method, crystals of the protein-inhibitor complex with the substrate analog pseudouridine
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in complex with the products, ribose 1-phosphate and uracil, at 1.8 A resolution. The biological unit is a hexamer with an alpha/beta monomeric fold. Residue His169 structurally aligns with Arg168 of the Escherichia coli uridine phosphorylase structure. A second active site residue, Lys162, is not present in previously determined uridine phosphorylase structures and interacts with O2 of uracil
crystallized at 18°C using the oil-microbatch method with PEG 4000 as a precipitant. A native data set is collected to 1.8 A resolution using synchrotron radiation. The crystal belongs to the monoclinic space group P2(1), with unit-cell parameters a = 58.83, b = 76.23, c = 103.86 A, beta = 91.3
crystals: monoclinic with dimensions of 0.13 * 0.13 * 0.07 mm, X-ray diffraction to 1.8 Å using synchrotron radiation at -173°C, belong to space group P2(1), asymmetric unit contains dimer with local pseudo-twofold symmetry, unit-cell parameters: a: 58.83, b: 76.23, c: 103.86, beta: 91.3°, oil-microbatch method: 1 week at 18°C, drop: 0.5 microlitre precipitant solution (27.5% (w/v) PEG 4000 in 100 mM HEPES-NaOH pH 7.5, 10 mM CaCl2) + 0.5 microlitre protein solution (21.7 mg/ml in 20 mM Tris-HCl pH8, 200 NaCl)
