2q9z

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[[Image:2q9z.gif|left|200px]]
 
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{{Structure
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==Trichodiene synthase: Complex with inorganic pyrophosphate resulting from the reaction with 2-fluorofarnesyl diphosphate==
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|PDB= 2q9z |SIZE=350|CAPTION= <scene name='initialview01'>2q9z</scene>, resolution 2.95&Aring;
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<StructureSection load='2q9z' size='340' side='right'caption='[[2q9z]], [[Resolution|resolution]] 2.95&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <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>
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<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>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Trichodiene_synthase Trichodiene synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.3.6 4.2.3.6] </span>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.95&#8491;</td></tr>
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|GENE= TRI5, TOX 5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5514 Fusarium sporotrichioides])
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<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>
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|DOMAIN=
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<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>
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|RELATEDENTRY=[[1jfa|1JFA]], [[1jfg|1JFG]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2q9z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q9z OCA], [http://www.ebi.ac.uk/pdbsum/2q9z PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2q9z RCSB]</span>
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== Function ==
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}}
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/q9/2q9z_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=2q9z ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''Trichodiene synthase: Complex with inorganic pyrophosphate resulting from the reaction with 2-fluorofarnesyl diphosphate'''
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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<ref>PMID:17678871</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2q9z" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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.
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*[[Trichodiene synthase|Trichodiene synthase]]
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== References ==
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==About this Structure==
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<references/>
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2Q9Z is a [[Single protein]] structure of sequence from [http://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].
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__TOC__
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</StructureSection>
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/17678871 17678871]
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[[Category: Fusarium sporotrichioides]]
[[Category: Fusarium sporotrichioides]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Trichodiene synthase]]
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[[Category: Cane DE]]
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[[Category: Cane, D E.]]
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[[Category: Christianson DW]]
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[[Category: Christianson, D W.]]
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[[Category: Coates RM]]
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[[Category: Coates, R M.]]
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[[Category: Koyama T]]
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[[Category: Koyama, T.]]
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[[Category: Vedula LS]]
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[[Category: Vedula, L S.]]
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[[Category: Zhao Y]]
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[[Category: Zhao, Y.]]
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[[Category: 2-fluorofarnesyl diphosphate]]
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[[Category: inorganic pyrophosphate]]
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[[Category: lyase]]
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[[Category: terpenoid synthase fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:46:45 2008''
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Current revision

Trichodiene synthase: Complex with inorganic pyrophosphate resulting from the reaction with 2-fluorofarnesyl diphosphate

PDB ID 2q9z

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