3D3W
Structure of L-Xylulose Reductase with bound coenzyme, phosphate and hydroxide.
Summary for 3D3W
| Entry DOI | 10.2210/pdb3d3w/pdb |
| Related | 1PR9 |
| Descriptor | L-xylulose reductase, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, PHOSPHATE ION, ... (5 entities in total) |
| Functional Keywords | l-xylulose reductase, uronate cycle, short-chain dehydrogenase/reductase(sdr) superfamily, glucose metabolism, acetylation, carbohydrate metabolism, membrane, nadp, oxidoreductase, xylose metabolism |
| Biological source | Homo sapiens (Human) More |
| Cellular location | Membrane; Peripheral membrane protein (By similarity): Q7Z4W1 Q7Z4W1 |
| Total number of polymer chains | 2 |
| Total formula weight | 53479.85 |
| Authors | Zhao, H.-T.,El-Kabbani, O. (deposition date: 2008-05-12, release date: 2009-04-21, Last modification date: 2024-11-13) |
| Primary citation | Zhao, H.T.,Endo, S.,Ishikura, S.,Chung, R.,Hogg, P.J.,Hara, A.,El-Kabbani, O. Structure/function analysis of a critical disulfide bond in the active site of L-xylulose reductase. Cell.Mol.Life Sci., 66:1570-1579, 2009 Cited by PubMed Abstract: 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 S-cysteinylation 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. PubMed: 19337691DOI: 10.1007/s00018-009-9065-y PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.87 Å) |
Structure validation
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