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1.5.1.33: pteridine reductase

This is an abbreviated version!
For detailed information about pteridine reductase, go to the full flat file.

Word Map on EC 1.5.1.33

Reaction

5,6,7,8-tetrahydrobiopterin
+ 2 NADP+ =
biopterin
+ 2 NADPH + 2 H+

Synonyms

Atu1130, EC 1.1.1.253, H region methotrexate resistance protein, LaPTR1, LbPTR1, LdPTR1, LmPTR1, LpPTR1, More, NADPH-dependent short-chain dehydrogenase/reductase pteridine reductase, NADPH-dihydropteridine reductase, PruA, pteridine reductase, pteridine reductase 1, pteridine reductase I, PTR1, reductase, dihydropteridine (reduced nicotinamide adenine dinucleotide phosphate), Tb-PR, TbPTR1, tcptr1

ECTree

     1 Oxidoreductases
         1.5 Acting on the CH-NH group of donors
             1.5.1 With NAD+ or NADP+ as acceptor
                1.5.1.33 pteridine reductase

Crystallization

Crystallization on EC 1.5.1.33 - pteridine reductase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 0.1 M MES pH 6.5, 10%(v/v) dioxane and 1.6 M ammonium sulfate
crystallized in complex with reduced cofactor and two different inhibitors
enzyme in ternary complex with NADPH and inhibitor 2,4,6-triaminoquinazoline in protein solution containing 10 mg/ml protein, 20 mM sodium acetate, pH 5.3, 1 mM NADPH, 1 mM 2,4,6-triaminoquinazoline, 20 mM DTT, and 1% DMSO, hanging drop vapour diffusion method, against equal volume of 0.002 ml of reservoir solution containing 11-14% PEG 5000, 100 mM sodium acetate, pH 5.5, and 40-140 mM calcium acetate, 20°C, thin grew clumps of thin fragile rods, cryopreservation in a solution of 0% reservoir solution and 30% glycerol, X-ray diffraction structure determination and analysis at 2.6 A resolution, molecular replacement
in complex with NADPH, and with NADPH and biopterin, 5,6-dihydrobiopterin, or 5,6,7,8-tetrahydrobiopterin as well as in complex with NADPH and inhibitors CB3717 or trimethoprim. Enzyme does not undergo major conformational changes to accomplish binding and processing of substrates. Quinazoline moiety of inhibotr CB3717 binds similarly to pterin of substrate
-
purified enzyme LmPtr1 in ternary complex with compounds 6-hydroxy-2-(3-hydroxyphenyl)-2,3-dihydro-4H-1-benzopyran-4-one and 2-(3,4-dihydroxyphenyl)-6-hydroxy-2,3-dihydro-4H-1-benzopyran-4-one, hanging drop vapour diffusion method, mixing of 0.002 ml of 12.5 mg/ml protein in 20 mM sodium acetate, pH 5.3, containing 1 mM NADPH, and 20 mM DTT, with 0.002 ml of reservoir solution containing 12% PEG 4600, 100 mM sodium acetate buffer pH 5.5 and 120-160 mM calcium acetate, equilibration against reservoir solution, at 20°C, for complex crystals the preformed crystals are soaked in a 2 mM inhibitor solution (dissolved in a 1:1 mixture of 1,4-dioxane and water) for 4.5 h, X-ray diffraction structure determination and analysis at 2.10-2.35 A resolution
purified recombinant enzyme in binary complex with NADPH and in ternary complex with NADPH and methotrexate, 0.02 ml of protein solution containing 20 mg/ml protein, 20 mM Tris-HCl, pH 7.0, mixed with 0.01 ml of a solution containing 4 mM NADPH, 4 mM methotrexate on ice for 1 h, then mixed with 0.01 ml of reservoir solution containing 28% 1,4-butanediol, 12.5 mM cetyl trimethyl ammonium chloride and 100 mM HEPES, pH 7.0, 5 days, 14°C, X-ray diffraction structure determination and analysis of flash frozen crystals at 2.8 A resolution, molecular replacement technique
purified enzyme TbPtr1 in ternary complex with compound 6-hydroxy-2-(3-hydroxyphenyl)-2,3-dihydro-4H-1-benzopyran-4-one, sitting drop vapor diffusion method, mixing of equal volumes of protein solution containing 6-10 mg/ml protein in 20 mM Tris-HCl, pH 7.5, and 10 mM DTT, with precipitant solution containing 1.5-2.5 M sodium acetate and 0.1 M sodium citrate, pH 5.0, equilibration against 0.6 ml of reservoir solution, at room temperature, several days, for complexed crystals are soaked in a 2 mM solution of the inhibitor (dissolved in a 1:1 mixture of 1,4-dioxane and water) for 4 h, X-ray diffraction structure determination and analysis at 1.70 A resolution
purified enzyme in a ternary complex with NADP(H) and inhibitor 2,4-diaminopyrimido[4,5-b]indol-6-ol, hanging drop vapor diffusion technique, using a precipitant solution composed of 2.0-2.5 M sodium acetate, 0.1 M sodium citrate, pH 5.0, a DMSO solution of the inhibitor compound is added to the cryoprotectant composed of the precipitant (enriched to 30% v/v glycerol) to a final concentration of 4 mM (the DMSO concentration is kept lower than 10% v/v), a few days at room temperature, X-ray diffraction structure determination and analysis at 1.30 A resolution, modelling
purified recombinant His-tagged TbPTR1, hanging drop vapour diffusion method, a few days at room temperature. Well-ordered monoclinic crystals are obtained using a precipitant solution composed of 2.0-2.5 M sodium acetate and 0.1 M sodium citrate, pH 5.0, the complex with PYR is obtained by the soaking technique, adding 3 mM of the compound (solubilized in DMSO) in crystallization drops containing preformed TbPTR1 crystals (without exceeding a DMSO/crystal solution ratio of 1:9) and incubating them overnight at room temperature, molecular replacement using a functional enzyme tetramer (PDB ID 6TBX) as searching model, and modelling