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| | <StructureSection load='2q9z' size='340' side='right'caption='[[2q9z]], [[Resolution|resolution]] 2.95Å' scene=''> | | <StructureSection load='2q9z' size='340' side='right'caption='[[2q9z]], [[Resolution|resolution]] 2.95Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2q9z]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Fussp Fussp]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q9Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Q9Z FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2q9z]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Fusarium_sporotrichioides Fusarium sporotrichioides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q9Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Q9Z FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</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]] 2.95Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1jfa|1jfa]], [[1jfg|1jfg]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TRI5, TOX 5 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5514 FUSSP])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Trichodiene_synthase Trichodiene synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.3.6 4.2.3.6] </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=2q9z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q9z OCA], [https://pdbe.org/2q9z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2q9z RCSB], [https://www.ebi.ac.uk/pdbsum/2q9z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2q9z 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=2q9z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q9z OCA], [https://pdbe.org/2q9z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2q9z RCSB], [https://www.ebi.ac.uk/pdbsum/2q9z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2q9z ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/TRI5_FUSSP TRI5_FUSSP]] TS is a member of the terpene cyclase group of enzymes. It catalyzes the isomerization and cyclization of farnesyl pyro-phosphate to form trichodiene, the first cyclic intermediate in the biosynthetic pathway for trichothecenes. It serves to branch trichothecene biosynthesis from the isoprenoid pathway.
| + | [https://www.uniprot.org/uniprot/TRI5_FUSSP TRI5_FUSSP] TS is a member of the terpene cyclase group of enzymes. It catalyzes the isomerization and cyclization of farnesyl pyro-phosphate to form trichodiene, the first cyclic intermediate in the biosynthetic pathway for trichothecenes. It serves to branch trichothecene biosynthesis from the isoprenoid pathway. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Fussp]] | + | [[Category: Fusarium sporotrichioides]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Trichodiene synthase]]
| + | [[Category: Cane DE]] |
| - | [[Category: Cane, D E]] | + | [[Category: Christianson DW]] |
| - | [[Category: Christianson, D W]] | + | [[Category: Coates RM]] |
| - | [[Category: Coates, R M]] | + | [[Category: Koyama T]] |
| - | [[Category: Koyama, T]] | + | [[Category: Vedula LS]] |
| - | [[Category: Vedula, L S]] | + | [[Category: Zhao Y]] |
| - | [[Category: Zhao, Y]] | + | |
| - | [[Category: 2-fluorofarnesyl diphosphate]]
| + | |
| - | [[Category: Inorganic pyrophosphate]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Terpenoid synthase fold]]
| + | |
| Structural highlights
Function
TRI5_FUSSP TS is a member of the terpene cyclase group of enzymes. It catalyzes the isomerization and cyclization of farnesyl pyro-phosphate to form trichodiene, the first cyclic intermediate in the biosynthetic pathway for trichothecenes. It serves to branch trichothecene biosynthesis from the isoprenoid pathway.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Trichodiene synthase is a terpenoid cyclase that catalyzes the cyclization of farnesyl diphosphate (FPP) to form the bicyclic sesquiterpene hydrocarbon trichodiene (89%), at least five sesquiterpene side products (11%), and inorganic pyrophosphate (PP(i)). Incubation of trichodiene synthase with 2-fluorofarnesyl diphosphate or 4-methylfarnesyl diphosphate similarly yields sesquiterpene mixtures despite the electronic effects or steric bulk introduced by substrate derivatization. The versatility of the enzyme is also demonstrated in the 2.85A resolution X-ray crystal structure of the complex with Mg(2+) (3)-PP(i) and the benzyl triethylammonium cation, which is a bulkier mimic of the bisabolyl carbocation intermediate in catalysis. Taken together, these findings show that the active site of trichodiene synthase is sufficiently flexible to accommodate bulkier and electronically-diverse substrates and intermediates, which could indicate additional potential for the biosynthetic utility of this terpenoid cyclase.
Exploring biosynthetic diversity with trichodiene synthase.,Vedula LS, Zhao Y, Coates RM, Koyama T, Cane DE, Christianson DW Arch Biochem Biophys. 2007 Oct 15;466(2):260-6. Epub 2007 Jun 28. PMID:17678871[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Vedula LS, Zhao Y, Coates RM, Koyama T, Cane DE, Christianson DW. Exploring biosynthetic diversity with trichodiene synthase. Arch Biochem Biophys. 2007 Oct 15;466(2):260-6. Epub 2007 Jun 28. PMID:17678871 doi:10.1016/j.abb.2007.06.016
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