2ps4

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[[Image:2ps4.jpg|left|200px]]
 
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==N225D trichodiene synthase==
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The line below this paragraph, containing "STRUCTURE_2ps4", creates the "Structure Box" on the page.
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<StructureSection load='2ps4' size='340' side='right'caption='[[2ps4]], [[Resolution|resolution]] 2.46&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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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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or leave the SCENE parameter empty for the default display.
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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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<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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{{STRUCTURE_2ps4| PDB=2ps4 | SCENE= }}
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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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==Overview==
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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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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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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</div>
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<div class="pdbe-citations 2ps4" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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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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*[[Trichodiene synthase|Trichodiene synthase]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[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: Lyase]]
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[[Category: Magnesium,ethylene glycol]]
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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 Sun May 4 13:42:40 2008''
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Current revision

N225D trichodiene synthase

PDB ID 2ps4

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