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| ==Crystal structure of homoisocitrate dehydrogenase from Schizosaccharomyces pombe== | | ==Crystal structure of homoisocitrate dehydrogenase from Schizosaccharomyces pombe== |
| <StructureSection load='3ty4' size='340' side='right' caption='[[3ty4]], [[Resolution|resolution]] 1.55Å' scene=''> | | <StructureSection load='3ty4' size='340' side='right'caption='[[3ty4]], [[Resolution|resolution]] 1.55Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[3ty4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Fission_yeast Fission yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TY4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TY4 FirstGlance]. <br> | | <table><tr><td colspan='2'>[[3ty4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe_972h- Schizosaccharomyces pombe 972h-]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TY4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TY4 FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.55Å</td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ty3|3ty3]]</td></tr>
| | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lys12, SPAC31G5.04 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284812 Fission yeast])</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=3ty4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ty4 OCA], [https://pdbe.org/3ty4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ty4 RCSB], [https://www.ebi.ac.uk/pdbsum/3ty4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ty4 ProSAT]</span></td></tr> |
| <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Homoisocitrate_dehydrogenase Homoisocitrate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.87 1.1.1.87] </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=3ty4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ty4 OCA], [http://pdbe.org/3ty4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ty4 RCSB], [http://www.ebi.ac.uk/pdbsum/3ty4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ty4 ProSAT]</span></td></tr> | |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
| | == Function == |
| == Publication Abstract from PubMed == | | [https://www.uniprot.org/uniprot/LYS12_SCHPO LYS12_SCHPO] |
| Homoisocitrate dehydrogenase (HICDH) catalyzes the conversion of homoisocitrate to 2-oxoadipate, the third enzymatic step in the alpha-aminoadipate pathway by which lysine is synthesized in fungi and certain archaebacteria. This enzyme represents a potential target for anti-fungal drug design. Here, we describe the first crystal structures of a fungal HICDH, including structures of an apoenzyme and a binary complex with a glycine tri-peptide. The structures illustrate the homology of HICDH with other beta-hydroxyacid oxidative decarboxylases and reveal key differences with the active site of Thermus thermophilus HICDH that provide insights into the differences in substrate specificity of these enzymes.
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| Crystal structure of homoisocitrate dehydrogenase from Schizosaccharomyces pombe.,Bulfer SL, Hendershot JM, Trievel RC Proteins. 2012 Feb;80(2):661-6. doi: 10.1002/prot.23231. Epub 2011 Nov 22. PMID:22105743<ref>PMID:22105743</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 3ty4" style="background-color:#fffaf0;"></div>
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Fission yeast]] | | [[Category: Large Structures]] |
| [[Category: Homoisocitrate dehydrogenase]] | | [[Category: Schizosaccharomyces pombe 972h-]] |
| [[Category: Bulfer, S L]] | | [[Category: Bulfer SL]] |
| [[Category: Hendershot, J M]] | | [[Category: Hendershot JM]] |
| [[Category: Trievel, R C]] | | [[Category: Trievel RC]] |
| [[Category: Amino-acid biosynthesis]]
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| [[Category: B-hydroxyacid oxidative decarboxylase]]
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| [[Category: Lysine biosynthesis]]
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| [[Category: Oxidoreductase]]
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