5evo

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==Structure of Dehydroascrobate Reductase from Pennisetum Americanum in complex with two non-native ligands, Acetate in the G-site and Glycerol in the H-site==
==Structure of Dehydroascrobate Reductase from Pennisetum Americanum in complex with two non-native ligands, Acetate in the G-site and Glycerol in the H-site==
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<StructureSection load='5evo' size='340' side='right' caption='[[5evo]], [[Resolution|resolution]] 2.51&Aring;' scene=''>
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<StructureSection load='5evo' size='340' side='right'caption='[[5evo]], [[Resolution|resolution]] 2.51&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5evo]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EVO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5EVO FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5evo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cenchrus_americanus Cenchrus americanus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EVO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EVO 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=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.51&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5evn|5evn]], [[5evp|5evp]], [[5evq|5evq]], [[5evr|5evr]], [[5evs|5evs]], [[5evt|5evt]], [[5evu|5evu]], [[5evv|5evv]], [[5evw|5evw]], [[5evx|5evx]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutathione_dehydrogenase_(ascorbate) Glutathione dehydrogenase (ascorbate)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.5.1 1.8.5.1] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5evo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5evo OCA], [https://pdbe.org/5evo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5evo RCSB], [https://www.ebi.ac.uk/pdbsum/5evo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5evo ProSAT]</span></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=5evo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5evo OCA], [http://pdbe.org/5evo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5evo RCSB], [http://www.ebi.ac.uk/pdbsum/5evo PDBsum]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/U5XYA0_CENAM U5XYA0_CENAM]
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Dehydroascorbate reductase (DHAR), a member of the glutathione-S-transferase (GST) family, reduces dehydroascorbate (DHA) to ascorbate (AsA; Vitamin-C) in a glutathione (GSH)-dependent manner and in doing so, replenishes the critical AsA pool of the cell. To understand the enzyme mechanism in detail, we determined the crystal structure of a plant DHAR from Pennisetum glaucum (PgDHAR) using Iodide-Single Anomalous Dispersion (SAD) and Molecular replacement methods, in two different space groups. Here, we show PgDHAR in complex with two non-native ligands, viz. an acetate bound at the G-site, which resembles the gamma-carboxyl moiety of GSH, and a glycerol at the H-site, which shares the backbone of AsA. We also show that, in the absence of bound native substrates, these non-native ligands help define the critical 'hook points' in the DHAR enzyme active site. Further, our data suggest that these non-native ligands can act as the logical bootstrapping points for iterative design of inhibitors/analogs for DHARs.
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Non-native ligands define the active site of Pennisetum glaucum (L.) R. Br dehydroascorbate reductase.,Krishna Das B, Kumar A, Maindola P, Mahanty S, Jain SK, Reddy MK, Arockiasamy A Biochem Biophys Res Commun. 2016 May 13;473(4):1152-7. doi:, 10.1016/j.bbrc.2016.04.031. Epub 2016 Apr 9. PMID:27067046<ref>PMID:27067046</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5evo" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Arockiasamy, A]]
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[[Category: Cenchrus americanus]]
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[[Category: Das, B K]]
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[[Category: Large Structures]]
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[[Category: Kumar, A O]]
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[[Category: Arockiasamy A]]
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[[Category: Dhar]]
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[[Category: Das BK]]
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[[Category: Non-native ligand]]
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[[Category: Kumar AO]]
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[[Category: Oxidoreductase]]
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Current revision

Structure of Dehydroascrobate Reductase from Pennisetum Americanum in complex with two non-native ligands, Acetate in the G-site and Glycerol in the H-site

PDB ID 5evo

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