3ty4: Difference between revisions
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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 [ | <table><tr><td colspan='2'>[[3ty4]] is a 2 chain structure with sequence from [https://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 [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='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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ty3|3ty3]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ty3|3ty3]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lys12, SPAC31G5.04 ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lys12, SPAC31G5.04 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284812 Fission yeast])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Homoisocitrate_dehydrogenase Homoisocitrate dehydrogenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.87 1.1.1.87] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <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> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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[[Category: Fission yeast]] | [[Category: Fission yeast]] | ||
[[Category: Homoisocitrate dehydrogenase]] | [[Category: Homoisocitrate dehydrogenase]] | ||
[[Category: Large Structures]] | |||
[[Category: Bulfer, S L]] | [[Category: Bulfer, S L]] | ||
[[Category: Hendershot, J M]] | [[Category: Hendershot, J M]] |
Revision as of 08:50, 13 July 2022
Crystal structure of homoisocitrate dehydrogenase from Schizosaccharomyces pombeCrystal structure of homoisocitrate dehydrogenase from Schizosaccharomyces pombe
Structural highlights
Publication Abstract from PubMedHomoisocitrate 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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