View source for 5zci


==Crystal structure of apo form of Xylose reductase from Debaryomyces nepalensis==
<StructureSection load='5zci' size='340' side='right'caption='[[5zci]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5zci]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Debaryomyces_nepalensis Debaryomyces nepalensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZCI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZCI FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</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=5zci FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zci OCA], [https://pdbe.org/5zci PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zci RCSB], [https://www.ebi.ac.uk/pdbsum/5zci PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zci ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0M4HL56_9ASCO A0A0M4HL56_9ASCO] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Aldose reductases (ARs) belonging to the aldo-keto reductase (AKR) superfamily catalyze the conversion of carbonyl substrates into their respective alcohols. Here we report the crystal structures of the yeast Debaryomyces nepalensis xylose reductase (DnXR, AKR2B10) in the apo form and as a ternary complex with a novel NADP-DTT adduct. Xylose reductase, a key enzyme in the conversion of xylose to xylitol, has several industrial applications. The enzyme displayed the highest catalytic efficiency for l-threose (138 +/- 7 mm(-1) .s(-1) ) followed by d-erythrose (30 +/- 3 mm(-1) .s(-1) ). The crystal structure of the complex reveals a 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. We hypothesize that 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. The interactions between DTT, a four-carbon sugar alcohol analog, and the enzyme are representative of a near-cognate product ternary complex and provide significant insights into the structural basis of aldose binding and specificity and the catalytic mechanism of ARs. DATABASE: Structural data are available in the PDB under the accession numbers 5ZCI and 5ZCM.

Crystal structure of yeast xylose reductase in complex with a novel NADP-DTT adduct provides insights into substrate recognition and catalysis.,Paidimuddala B, Mohapatra SB, Gummadi SN, Manoj N FEBS J. 2018 Sep 30. doi: 10.1111/febs.14667. PMID:30269423<ref>PMID:30269423</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5zci" style="background-color:#fffaf0;"></div>

==See Also==
*[[Aldose reductase 3D structures|Aldose reductase 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Debaryomyces nepalensis]]
[[Category: Large Structures]]
[[Category: Manoj N]]