2ps4

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[[Image:2ps4.jpg|left|200px]]
 
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{{Structure
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==N225D trichodiene synthase==
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|PDB= 2ps4 |SIZE=350|CAPTION= <scene name='initialview01'>2ps4</scene>, resolution 2.46&Aring;
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<StructureSection load='2ps4' size='340' side='right'caption='[[2ps4]], [[Resolution|resolution]] 2.46&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>
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<table><tr><td colspan='2'>[[2ps4]] 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=2PS4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PS4 FirstGlance]. <br>
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|ACTIVITY= [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]
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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]] 2.46&#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></td></tr>
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}}
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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=2ps4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ps4 OCA], [https://pdbe.org/2ps4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ps4 RCSB], [https://www.ebi.ac.uk/pdbsum/2ps4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ps4 ProSAT]</span></td></tr>
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</table>
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== Function ==
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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/ps/2ps4_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=2ps4 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 from Fusarium sporotrichioides contains two metal ion-binding motifs required for the cyclization of farnesyl diphosphate: the "aspartate-rich" motif D(100)DXX(D/E) that coordinates to Mg2+A and Mg2+C, and the "NSE/DTE" motif N(225)DXXSXXXE that chelates Mg2+B (boldface indicates metal ion ligands). Here, we report steady-state kinetic parameters, product array analyses, and X-ray crystal structures of trichodiene synthase mutants in which the fungal NSE motif is progressively converted into a plant-like DDXXTXXXE motif, resulting in a degradation in both steady-state kinetic parameters and product specificity. Each catalytically active mutant generates a different distribution of sesquiterpene products, and three newly detected sesquiterpenes are identified. In addition, the kinetic and structural properties of the Y295F mutant of trichodiene synthase were found to be similar to those of the wild-type enzyme, thereby ruling out a proposed role for Y295 in catalysis.
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'''N225D trichodiene synthase'''
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Structural and mechanistic analysis of trichodiene synthase using site-directed mutagenesis: probing the catalytic function of tyrosine-295 and the asparagine-225/serine-229/glutamate-233-Mg2+B motif.,Vedula LS, Jiang J, Zakharian T, Cane DE, Christianson DW Arch Biochem Biophys. 2008 Jan 15;469(2):184-94. Epub 2007 Oct 30. PMID:17996718<ref>PMID:17996718</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 2ps4" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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Trichodiene synthase from Fusarium sporotrichioides contains two metal ion-binding motifs required for the cyclization of farnesyl diphosphate: the "aspartate-rich" motif D(100)DXX(D/E) that coordinates to Mg2+A and Mg2+C, and the "NSE/DTE" motif N(225)DXXSXXXE that chelates Mg2+B (boldface indicates metal ion ligands). Here, we report steady-state kinetic parameters, product array analyses, and X-ray crystal structures of trichodiene synthase mutants in which the fungal NSE motif is progressively converted into a plant-like DDXXTXXXE motif, resulting in a degradation in both steady-state kinetic parameters and product specificity. Each catalytically active mutant generates a different distribution of sesquiterpene products, and three newly detected sesquiterpenes are identified. In addition, the kinetic and structural properties of the Y295F mutant of trichodiene synthase were found to be similar to those of the wild-type enzyme, thereby ruling out a proposed role for Y295 in catalysis.
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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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2PS4 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=2PS4 OCA].
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__TOC__
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</StructureSection>
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==Reference==
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Structural and mechanistic analysis of trichodiene synthase using site-directed mutagenesis: probing the catalytic function of tyrosine-295 and the asparagine-225/serine-229/glutamate-233-Mg2+B motif., Vedula LS, Jiang J, Zakharian T, Cane DE, Christianson DW, Arch Biochem Biophys. 2008 Jan 15;469(2):184-94. Epub 2007 Oct 30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17996718 17996718]
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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: Vedula LS]]
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[[Category: Vedula, L S.]]
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[[Category: EDO]]
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[[Category: MG]]
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[[Category: ethylene glycol]]
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[[Category: lyase]]
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[[Category: magnesium]]
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[[Category: nse/dte motif]]
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[[Category: site-directed mutagenesis]]
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[[Category: terpenoid synthase fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:16:44 2008''
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Current revision

N225D trichodiene synthase

PDB ID 2ps4

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