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| - | | + | #REDIRECT [[6bii]] This PDB entry is obsolete and replaced by 6bii |
| - | ==Ternary Crystal Structure of Pyrococcus yayanosii Glyoxylate Hydroxypyruvate Reductase in presence of D-glycerate==
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| - | <StructureSection load='5aow' size='340' side='right' caption='[[5aow]], [[Resolution|resolution]] 2.00Å' scene=''>
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| - | == Structural highlights ==
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| - | <table><tr><td colspan='2'>[[5aow]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AOW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AOW FirstGlance]. <br>
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| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DGY:(2R)-2,3-DIHYDROXYPROPANOIC+ACID'>DGY</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
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| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5aov|5aov]]</td></tr>
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| - | <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=5aow FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aow OCA], [http://pdbe.org/5aow PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5aow RCSB], [http://www.ebi.ac.uk/pdbsum/5aow PDBsum]</span></td></tr>
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| - | </table>
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| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | Glyoxylate accumulation within cells is highly toxic. In humans, it is associated with hyperoxaluria type 2 (PH2) leading to renal failure. The glyoxylate content within cells is regulated by the NADPH/NADH dependent glyoxylate/hydroxypyruvate reductases (GRHPR). These are highly conserved enzymes with a dual activity as they are able to reduce glyoxylate to glycolate and to convert hydroxypyruvate into D-glycerate. Despite the determination of high-resolution X-ray structures, the substrate recognition mode of this class of enzymes remains unclear. We determined the structure at 2.0 A resolution of a thermostable GRHPR from Archaea as a ternary complex in the presence of D-glycerate and NADPH. This shows a binding mode conserved between human and archeal enzymes. We also determined the first structure of GRHPR in presence of glyoxylate at 1.40 A resolution. This revealed the pivotal role of Leu53 and Trp138 in substrate trafficking. These residues act as gatekeepers at the entrance of a tunnel connecting the active site to protein surface. Taken together, these results allowed us to propose a general model for GRHPR mode of action.
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| - | New insights into the mechanism of substrates trafficking in Glyoxylate/Hydroxypyruvate reductases.,Lassalle L, Engilberge S, Madern D, Vauclare P, Franzetti B, Girard E Sci Rep. 2016 Feb 11;6:20629. doi: 10.1038/srep20629. PMID:26865263<ref>PMID:26865263</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 5aow" style="background-color:#fffaf0;"></div>
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| - | == References ==
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| - | <references/>
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| - | __TOC__
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| - | </StructureSection>
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| - | [[Category: Girard, E]]
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| - | [[Category: Lassalle, L]]
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| - | [[Category: Archaea]]
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| - | [[Category: D-glycerate]]
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| - | [[Category: Glyoxylate hydroxypyruvate reductase]]
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| - | [[Category: Oxidoreductase]]
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