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| | <StructureSection load='5iqy' size='340' side='right'caption='[[5iqy]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='5iqy' size='340' side='right'caption='[[5iqy]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5iqy]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cenam Cenam]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IQY OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5IQY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5iqy]] 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=5IQY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IQY FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> |
| - | <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> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5iqy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5iqy OCA], [http://pdbe.org/5iqy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5iqy RCSB], [http://www.ebi.ac.uk/pdbsum/5iqy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5iqy ProSAT]</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=5iqy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5iqy OCA], [https://pdbe.org/5iqy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5iqy RCSB], [https://www.ebi.ac.uk/pdbsum/5iqy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5iqy ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/U5XYA0_CENAM U5XYA0_CENAM] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cenam]] | + | [[Category: Cenchrus americanus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Arockiasamy, A]] | + | [[Category: Arockiasamy A]] |
| - | [[Category: Das, B K]] | + | [[Category: Das BK]] |
| - | [[Category: Kumar, A]] | + | [[Category: Kumar A]] |
| - | [[Category: Manidola, P]] | + | [[Category: Manidola P]] |
| - | [[Category: Dehydroascorbate reductase]]
| + | |
| - | [[Category: Iodide-sad method]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
U5XYA0_CENAM
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Krishna Das B, Kumar A, Maindola P, Mahanty S, Jain SK, Reddy MK, Arockiasamy A. Non-native ligands define the active site of Pennisetum glaucum (L.) R. Br dehydroascorbate reductase. 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 doi:http://dx.doi.org/10.1016/j.bbrc.2016.04.031
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