1.1.1.431: D-xylose reductase (NADPH)
This is an abbreviated version!
For detailed information about D-xylose reductase (NADPH), go to the full flat file.
Reaction
Synonyms
ALR1, Cb-XR, CbXR, CtXR, D-xylose reductase, D-xylose reductase 1, D-xylose reductase 2, D-xylose reductase 3, DnXR, GRE3, monospecific xylose reductase, More, msXR, NAD(P)H-dependent D-xylose reductase, NAD(P)H-dependent xylose reductase, NADPH dependent D-xylose reductase, NADPH-dependent D-xylose reductase II,III, NADPH-dependent xylose reductase, NADPH-preferring xylose reductase, NRRL3_10868, SsXR, Texr, TrxR, XR1, XR2, XR3, XRTL, XYL1, xylose reductase, xyr8, XyrA, XyrB
ECTree
1.1.1.431 D-xylose reductase (NADPH)Advanced search results
results (
results (Crystallization
Crystallization on EC 1.1.1.431 - D-xylose reductase (NADPH)
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CRYSTALLIZATION (Commentary) 
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour diffusion method, to 2.91 A resolution. Unit cell belongs to space group P31 or P32, presence of four XR molecules in the asymmetric unit, with 68.0% solvent content
hanging-drop vapour-diffusion method. X-ray diffraction data from xylose reductase crystals at 2.91 A resolution, the unit cell belongs to space group P3(1) or P3(2). Preliminary analysis indicates the presence of four xylose reductase molecules in the asymmetric unit, with 68.0% solvent content
purified xylose reductase (DnXR) in the apoform and as a ternary complex with a NADP-DTT adduct, covalent linkage between the C4N atom of the nicotinamide ring of the cosubstrate and the S1 sulfur atom of DTT and provides the first structural evidence for a protein mediated NADP-low-molecular-mass thiol adduct, the formation of the adduct is facilitated by an in-crystallo Michael addition of the DTT thiolate to the specific conformation of bound NADPH in the active site of DnXR. Hanging drop vapor diffusion method, mixing of 0.001 ml of 15 mg/ml protein in 20 mM Tris/HCl, pH 7.5, with 0.001 ml of reservoir solution containing 24% PEG 4000, 0.1 M sodium citrate, pH 6.2, and 0.15 M ammonium acetate, 20°C, for the complex crystals, 10 mM NADPH and 10 mM DTT are added to the protein solution and a reservoir solution containing 22% PEG 3350, 0.1 M HEPES, pH 7.5, and 0.2 M ammonium sulfate is used, X-ray diffraction structure determination and analysis at 1.7-2.0 A resolution, modeling
construction of a 3D structural model. The favourable binding modes for both cofactors NAD(H) and NADP(H) are obtained. The cofactor binding site is composed of a hydrophilic pocket, a hydrophobic pocket as well as a linker channel between the aforementioned two pockets. The hydrophilic pocket could recognize the nicotinamide moiety of the cofactors by hydrogen bonding networks, while the hydrophobic pocket functions to position the adenine moiety of the cofactors by hydrophobic and pi-pi stacking interactions. The linker channel contains some key residues for ligand-binding, their mutation could have impact to the catalytic specificity
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purified enzyme in apoform and in complex with NADPH, X-ray diffraction structure determination and analysis at 1.95-2.0 A resolution, the apoform structure is determined by molecular replacement using the structure of xylose reductase from Candida tenuis (CtXR, PDB ID 1Z9A) as a search model, the structure of SsXR in complex with NADPH is determined by molecular replacement using the crystal structure of the apoform of SsXR (PDB ID 5Z6U), model building
the purified N309D mutant is crystallized by the hanging-drop vapour-diffusion method at 25°C. The best-diffracting crystals are grown using a well solution consisting of 2.1 M (NH4)2SO4, 100 mM sodium acetate and 100 mM sodium citrate, pH 6.4. Comparison of the 2.4 A X-ray crystal structure of mutant N309D bound to NAD+ with the previous structure of the wild-type holoenzyme reveals no major structural perturbations
