5z6t
From Proteopedia
(Difference between revisions)
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<StructureSection load='5z6t' size='340' side='right' caption='[[5z6t]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='5z6t' size='340' side='right' caption='[[5z6t]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5z6t]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Z6T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Z6T FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5z6t]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Picst Picst]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Z6T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Z6T FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">XYL1, PICST_89614 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=322104 PICST])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/D-xylose_reductase D-xylose reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.307 1.1.1.307] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/D-xylose_reductase D-xylose reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.307 1.1.1.307] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5z6t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5z6t OCA], [http://pdbe.org/5z6t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5z6t RCSB], [http://www.ebi.ac.uk/pdbsum/5z6t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5z6t ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5z6t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5z6t OCA], [http://pdbe.org/5z6t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5z6t RCSB], [http://www.ebi.ac.uk/pdbsum/5z6t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5z6t ProSAT]</span></td></tr> | ||
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/XYL1_PICST XYL1_PICST]] Reduces D-xylose into xylitol. Has a preference for NADPH, but can also utilize NADH as cosubstrate.<ref>PMID:3921014</ref> | [[http://www.uniprot.org/uniprot/XYL1_PICST XYL1_PICST]] Reduces D-xylose into xylitol. Has a preference for NADPH, but can also utilize NADH as cosubstrate.<ref>PMID:3921014</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Lignocellulosic biomass, of which D-xylose accounts for approximately 35% of the total sugar, has attracted attention as a future energy source for biofuel. To elucidate molecular mechanism of D-xylose utilization, we determined the crystal structure of D-xylose reductase from Schefferzomyces stipitis (SsXR) at a 1.95 A resolution. We also determined the SsXR structure in complex with the NADPH cofactor and revealed that the protein undergoes an open/closed conformation change upon NADPH binding. The substrate binding pocket of SsXR is somewhat hydrophobic, which seems to result in low binding affinity to the substrate. Phylogenetic tree analysis showed that AKR enzymes annotated with bacterial/archaeal XRs belonged to uncharacterized AKR families and might have no XR function, and yeast/fungi derived enzymes, which belong to the same group with SsXR, can be candidates for XR to increase xylose consumption. | ||
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| + | Structural insight into D-xylose utilization by xylose reductase from Scheffersomyces stipitis.,Son HF, Lee SM, Kim KJ Sci Rep. 2018 Nov 28;8(1):17442. doi: 10.1038/s41598-018-35703-x. PMID:30487522<ref>PMID:30487522</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5z6t" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: D-xylose reductase]] | [[Category: D-xylose reductase]] | ||
| + | [[Category: Picst]] | ||
[[Category: Kim, K J]] | [[Category: Kim, K J]] | ||
[[Category: Son, H F]] | [[Category: Son, H F]] | ||
Revision as of 08:46, 19 December 2018
Crystal strcuture of D-xylose reductase from Scheffersomyces stipitis in complex with NADPH
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