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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]] 1.55&Aring;' scene=''>
<StructureSection load='3ty4' size='340' side='right' caption='[[3ty4]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
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<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='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='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>
<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>
<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://www.rcsb.org/pdb/explore.do?structureId=3ty4 RCSB], [http://www.ebi.ac.uk/pdbsum/3ty4 PDBsum]</span></td></tr>
<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;">
== Publication Abstract from PubMed ==
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.
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>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3ty4" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Revision as of 12:27, 11 August 2016

Crystal structure of homoisocitrate dehydrogenase from Schizosaccharomyces pombeCrystal structure of homoisocitrate dehydrogenase from Schizosaccharomyces pombe

Structural highlights

3ty4 is a 2 chain structure with sequence from Fission yeast. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:lys12, SPAC31G5.04 (Fission yeast)
Activity:Homoisocitrate dehydrogenase, with EC number 1.1.1.87
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

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.

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

  1. ↑ Bulfer SL, Hendershot JM, Trievel RC. Crystal structure of homoisocitrate dehydrogenase from Schizosaccharomyces pombe. Proteins. 2011 Oct 24. doi: 10.1002/prot.23231. PMID:22105743 doi:10.1002/prot.23231

3ty4, resolution 1.55Å

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