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1.17.1.8: 4-hydroxy-tetrahydrodipicolinate reductase

This is an abbreviated version!
For detailed information about 4-hydroxy-tetrahydrodipicolinate reductase, go to the full flat file.

Word Map on EC 1.17.1.8

Reaction

(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate
+
NAD(P)+
 +
H2O
=
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate
 +
NAD(P)H
 +
H+

Synonyms

AbDHDPR, CRR1, DapB, DHDP reductase, DHDPR, DHPR, dihydrodipicolinate reductase, dihydrodipicolinate reductase-like protein, dihydrodipicolinic acid reductase, EC 1.3.1.26, MRSA-DHDPR, reductase, dihydrodipicolinate

ECTree

     1 Oxidoreductases
         1.17 Acting on CH or CH2 groups
             1.17.1 With NAD+ or NADP+ as acceptor
                1.17.1.8 4-hydroxy-tetrahydrodipicolinate reductase

Crystallization

Crystallization on EC 1.17.1.8 - 4-hydroxy-tetrahydrodipicolinate reductase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals are grown using the hanging-drop vapour-diffusion method. The crystals belong to the orthorhombic space group P222, with unit-cell parameters a: 80.0, b: 100.8, c: 147.6 A, and contain four molecules in the asymmetric unit
-
vapour-diffusion method
sitting-drop vapor-diffusion, protein crystals are grown in conditions consisting of 5%(w/v) PEG 4000, 200 mM sodium acetate, 100 mM sodium citrate tribasic pH 5.5 and are shown to diffract to about 2.3 A resolution. They belong to space group P4(3)22, with unit cell parameters a = 109.38, b = 109.38, c = 176.95 A
crystal structure of the enzyme in the apoform and in complex with its cofactor NADP+, determined at 2.5 A resolution. The crystal belongs to the I4(1)22 space group, and the asymmetric unit of the crystal contains two CgDapB molecules
crystal structure of the enzyme in the apoform and in complex with its cofactor NADP+, hanging-drop vapor-diffusion method at 20°C, crystal structure of the enzyme is determined at 2.5 A resolution
hanging drop vapour diffusion method, crystal structure x-ray analysis and binding study with NADPH, NADH, 3-acetyl-NADH, and reduced nicotinamide hypoxanthine dinucleotide phosphate and other pyridine nucleotide derivatives in complex with the enzyme
R-factor 18.6%, structure model of enzyme complexed with NADPH, analysis of cofactor binding site
-
R-factor 21.4%, three-dimensional structure analysis , homotetramer with 3 molecules of NADH, 3 molecules of inhibitor 2,6-pyridinedicarboxylic acid, 1 phosphate ion and 186 water molecules per asymmetric unit in the model
purified recombinant wild-type enzyme in ternary complex with inhibitor 2,6-pyridinedicarboxylate and NADH or NADPH, hanging drop vapour diffusion method, room temperature, 0.003 ml protein solution containing 20 mg/ml enzyme, 2 mM NADH or NADPH, and 30 mM 2,6-pyridinedicarboxylate, mixed with 0.003 ml precipitant solution containing 2.2 M ammonium sulfate, 0.1 M HEPES, pH 7.5, 3% PEG 400, 3 days, X-ray diffraction strcuture determination at 16°C and 2.2 A resolution and analysis
sitting-drop vapour-diffusion method
purified recombinant enzyme, sitting-drop vapour-diffusion method, 100 ml drops of 9-10 mg/ml protein in 20 mM Tris-HCl, pH 8.0, and 150 mM NaCl with 10 mM 2,6-PDC and 10 mM NADPH are mixed with 100 ml of reservoir solution containing 2.4 M ammonium sulfate, 0.2 M sodium fluoride, and 0.1 M bis-tris propane, pH 7.5, and ethanol added to 10% v/v, 8°C, X-ray diffraction structure determination and analysis at 3.65 A resolution
-
using 2.0 M ammonium sulfate and 0.2 M sodium acetate pH 4.5
crystal structure is determined at 1.92 A