3d3w

Structure of L-Xylulose Reductase with bound coenzyme, phosphate and hydroxide.

spinqualitylabelsall models 3d3w, resolution 1.87Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3d3w is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: NAP, PO4 NonStd Res: CSO Related: 1pr9 Gene: DCXR (HUMAN) Activity: L-xylulose reductase, with EC number 1.1.1.10 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease [DCXR_HUMAN] Note=The enzyme defect in pentosuria has been shown to involve L-xylulose reductase. Essential pentosuria is an inborn error of metabolism characterized by the excessive urinary excretion of the pentose L-xylulose. Function [DCXR_HUMAN] Catalyzes the NADPH-dependent reduction of several pentoses, tetroses, trioses, alpha-dicarbonyl compounds and L-xylulose. Participates in the uronate cycle of glucose metabolism. May play a role in the water absorption and cellular osmoregulation in the proximal renal tubules by producing xylitol, an osmolyte, thereby preventing osmolytic stress from occurring in the renal tubules. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed L: -Xylulose reductase (XR) is involved in water re-absorption and cellular osmoregulation. The crystal structure of human XR complemented with site-directed mutagenesis (Cys138Ala) indicated that the disulfide bond in the active site between Cys138 and Cys150 is unstable and may affect the reactivity of the enzyme. The effects of reducing agents on the activities of the wild-type and mutant enzymes indicated the reversibility of disulfide-bond formation, which resulted in three-fold decrease in catalytic efficiency. Furthermore, the addition of cysteine (>2 mM) inactivated human XR and was accompanied by a 10-fold decrease in catalytic efficiency. TOF-MS analysis of the inactivated enzyme showed the Scysteinylation of Cys138 in the wild-type and Cys150 in the mutant enzymes. Thus, the action of human XR may be regulated by cellular redox conditions through reversible disulfide-bond formation and by S-cysteinylation. Structure/function analysis of a critical disulfide bond in the active site of L: -xylulose reductase.,Zhao HT, Endo S, Ishikura S, Chung R, Hogg PJ, Hara A, El-Kabbani O Cell Mol Life Sci. 2009 Apr 2. PMID:19337691 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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