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==Homocitrate Synthase Lys4 bound to 2-OG==
==Homocitrate Synthase Lys4 bound to 2-OG==
<StructureSection load='3ivt' size='340' side='right' caption='[[3ivt]], [[Resolution|resolution]] 2.67&Aring;' scene=''>
<StructureSection load='3ivt' size='340' side='right'caption='[[3ivt]], [[Resolution|resolution]] 2.67&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3ivt]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cbs_356 Cbs 356]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IVT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3IVT FirstGlance]. <br>
<table><tr><td colspan='2'>[[3ivt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IVT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IVT FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AKG:2-OXOGLUTARIC+ACID'>AKG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.67&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ivs|3ivs]], [[3ivu|3ivu]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AKG:2-OXOGLUTARIC+ACID'>AKG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lys4, SPBC1105.02c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4896 CBS 356])</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=3ivt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ivt OCA], [https://pdbe.org/3ivt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ivt RCSB], [https://www.ebi.ac.uk/pdbsum/3ivt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ivt 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/Homocitrate_synthase Homocitrate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.3.14 2.3.3.14] </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=3ivt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ivt OCA], [http://pdbe.org/3ivt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ivt RCSB], [http://www.ebi.ac.uk/pdbsum/3ivt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ivt ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HOSM_SCHPO HOSM_SCHPO]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3ivt ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3ivt ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Homocitrate synthase (HCS) catalyzes the first and committed step in lysine biosynthesis in many fungi and certain Archaea and is a potential target for antifungal drugs. Here we report the crystal structure of the HCS apoenzyme from Schizosaccharomyces pombe and two distinct structures of the enzyme in complex with the substrate 2-oxoglutarate (2-OG). The structures reveal that HCS forms an intertwined homodimer stabilized by domain-swapping between the N- and C-terminal domains of each monomer. The N-terminal catalytic domain is composed of a TIM barrel fold in which 2-OG binds via hydrogen bonds and coordination to the active site divalent metal ion, whereas the C-terminal domain is composed of mixed alpha/beta topology. In the structures of the HCS apoenzyme and one of the 2-OG binary complexes, a lid motif from the C-terminal domain occludes the entrance to the active site of the neighboring monomer, whereas in the second 2-OG complex the lid is disordered, suggesting that it regulates substrate access to the active site through its apparent flexibility. Mutations of the active site residues involved in 2-OG binding or implicated in acid-base catalysis impair or abolish activity in vitro and in vivo. Together, these results yield new insights into the structure and catalytic mechanism of HCSs and furnish a platform for developing HCS-selective inhibitors.


Crystal structure and functional analysis of homocitrate synthase, an essential enzyme in lysine biosynthesis.,Bulfer SL, Scott EM, Couture JF, Pillus L, Trievel RC J Biol Chem. 2009 Dec 18;284(51):35769-80. Epub . PMID:19776021<ref>PMID:19776021</ref>
==See Also==
 
*[[Homocitrate synthase|Homocitrate synthase]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3ivt" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Cbs 356]]
[[Category: Large Structures]]
[[Category: Homocitrate synthase]]
[[Category: Schizosaccharomyces pombe]]
[[Category: Bulfer, S L]]
[[Category: Bulfer SL]]
[[Category: Couture, J F]]
[[Category: Couture J-F]]
[[Category: Pillus, L]]
[[Category: Pillus L]]
[[Category: Scott, E M]]
[[Category: Scott EM]]
[[Category: Trievel, R C]]
[[Category: Trievel RC]]
[[Category: Amino-acid biosynthesis]]
[[Category: Claisen condensation]]
[[Category: Lysine biosynthesis]]
[[Category: Metalloprotein]]
[[Category: Mitochondrion]]
[[Category: Tim barrel]]
[[Category: Transferase]]
[[Category: Transit peptide]]
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