Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
the crystal structure of the ternary complex 2,4-dienoyl-CoA reductase-trans-2,trans-4-hexadienoyl-CoA-NADP+ reveals that the carbonyl oxygen of the substrate accepts a hydrogen bond from general acid Y199 and also N148
15 mg/ml purified recombinant enzyme, hanging drop vapour diffusion method, reservoir solution: 30% PEG 5000 monomethyl ether, 0.2 M sodium acetate, 0.1 M ammonium sulfate, 0.1 M 3-(N-morpholino)ethane sulfonic acid, pH 6.5, precipitant solution: 18% PEG 5000 monomethyl ether, 180 mM sodium acetate, 90 mM ammonium sulfate, 90 mM 3-(N-morpholino)ethane sulfonic acid, mixture in a ratio 1:1.5, 1 week, no cryoprotection, X-ray diffraction structure determination and analysis at 2.2 A resolution, heavy atom derivatives
the crystal structure of a ternary complex of peroxisomal 2,4-dienoyl CoA reductases (pDCR) with hexadienoyl CoA and NADP is described. The structure of pDCR refined to 1.84 A resolution reveals the absence of the tyrosine-serine pair seen in the active site of mitochondrial DCR. Instead, aspartate hydrogen-bonded to the Calpha hydroxyl via a water molecule perturbs the water molecule for protonation of the substrate
wild-type and selenomethionine enzyme, 0.001 ml of protein and of reservoir solution, the latter containing 16% PEG 4000 w/v, 0.18 M ammonium sulfate, 80 mM sodium acetate, pH 4.6, 20% glycerol, addition of 30% ethylene glycol and 4 mM NADP+ for the binary complex of enzyme with NADP+, and 120 mM substrate for the ternary complex of enzyme with NADP+ and substrate trans-trans-2,4-dienoyl-CoA, X-ray diffraction structure determination and analysis at 2.1 A and 1.75 A resolution, respectively