L-threonine 3-dehydrogenase

This is an abbreviated version, for detailed information about L-threonine 3-dehydrogenase, go to the full flat file.




CLOST_1621, L-ThrDH, L-threonine dehydrogenase, More, orf382, TDG, TDH, Thr dehydrogenase, ThrDH, threonine 3-dehydrogenase, threonine dehydrogenase


     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
       L-threonine 3-dehydrogenase


Crystallization on EC - L-threonine 3-dehydrogenase

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hanging drop vapor diffusion method, using 20% (w/v) PEG 3350 and 0.2 M CaCl2
apo form, in complex with NAD+ and glycerol, or with only NAD+, sitting drop vapor diffusion method, using 0.1 M HEPES (pH 7.0), 10% (w/v) PEG 4000, 10% (v/v) 2-propanol, or 0.2 M NaCl, 0.1 M HEPES (pH 7.5), 25% (w/v) PEG3350
purified recombinant enzyme, hanging drop vapour diffusion method, 4C, 10 mg/ml protein in 50 mM Tris-HCl, pH 7.5, 0.0015 ml of protein and reservoir solution are mixed, the reservoir solution contains 0.2 M NaCl, 0.1 M HEPES, pH 7.5, and 40% v/v PEG 400, 5 days, X-ray diffraction structure determination and preliminary analysis at 2.2 A resolution
selenomethionine-substituted enzyme, 10 mg/ml protein in 50 mM Tris-HCl buffer, pH 7.5, hanging-drop vapor-diffusion method at 4C, mixing of 0.0015 ml of each, protein and reservoir solution, the latter containing 0.2 M sodium chloride, 0.1 M HEPES buffer, pH 7.5, and 40% v/v PEG 400, five days, X-ray diffraction structure determination and analysis, single wavelength anomalous diffraction method
at room temperature using hanging-drop vapour diffusion method, at 2.4 A resolution. The enzyme is a homotetramer, each monomer consisting of 350 amino acids that form two domains, a catalytic domain and a NAD+-binding domain, which contains an alpha/beta Rossmann fold motif. An extended twelve-stranded beta-sheet is formed by the association of pairs of monomers in the tetramer
by hanging-drop vapour-diffusion method, to 2.6 A resolution. Crystals grow in the tetragonal space group P43212, with unit-cell parameters a=b=124.5, c=271.1 A. There are four molecules in the asymmetric unit of the crystal
purified wild-type enzyme or enzyme mutant Y137F in complex with NAD+ and L-3-hydroxynorvaline or pyruvate or L-threonine, sitting drop vapor diffusion method, mixing of 0.001 ml of 40 mg/ml wild-type or 25 mg/ml mutant enzyme, and 1 mM NAD+ mixed with 0.001 ml of 100 mM cacodylate buffer, pH 6.4, 50% v/v 2-methyl-2,4-pentandiol, and 5% w/v PEG 8000, 20C, crystals of ligand-bound wild-type or mutant enzymes by soaking the crystals in reservoir solution containing 0.3 M pyruvate for 2 h, or 0.1ML-threonine for 8 h or 0.1MDL-3-hydroxynorvaline for 7 h, respectively, X-ray diffraction structure determination and analysis at 1.77-2.07 A resolution, molecular replacement