3d3w
From Proteopedia
(Difference between revisions)
| (8 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Structure of L-Xylulose Reductase with bound coenzyme, phosphate and hydroxide.== | |
| + | <StructureSection load='3d3w' size='340' side='right'caption='[[3d3w]], [[Resolution|resolution]] 1.87Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3d3w]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D3W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3D3W FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1pr9|1pr9]]</div></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DCXR ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/L-xylulose_reductase L-xylulose reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.10 1.1.1.10] </span></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3d3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d3w OCA], [https://pdbe.org/3d3w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3d3w RCSB], [https://www.ebi.ac.uk/pdbsum/3d3w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3d3w ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Disease == | ||
| + | [[https://www.uniprot.org/uniprot/DCXR_HUMAN 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 == | ||
| + | [[https://www.uniprot.org/uniprot/DCXR_HUMAN 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 == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d3/3d3w_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3d3w ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:19337691</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 3d3w" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Human]] | ||
| + | [[Category: L-xylulose reductase]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: El-Kabbani, O]] | ||
| + | [[Category: Zhao, H T]] | ||
| + | [[Category: Acetylation]] | ||
| + | [[Category: Carbohydrate metabolism]] | ||
| + | [[Category: Glucose metabolism]] | ||
| + | [[Category: Membrane]] | ||
| + | [[Category: Nadp]] | ||
| + | [[Category: Oxidoreductase]] | ||
| + | [[Category: Uronate cycle]] | ||
| + | [[Category: Xylose metabolism]] | ||
Current revision
Structure of L-Xylulose Reductase with bound coenzyme, phosphate and hydroxide.
| |||||||||||
