1dgp

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[[Image:1dgp.jpg|left|200px]]
 
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{{Structure
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==ARISTOLOCHENE SYNTHASE FARNESOL COMPLEX==
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|PDB= 1dgp |SIZE=350|CAPTION= <scene name='initialview01'>1dgp</scene>, resolution 2.8&Aring;
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<StructureSection load='1dgp' size='340' side='right'caption='[[1dgp]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=FOH:FARNESOL'>FOH</scene>
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<table><tr><td colspan='2'>[[1dgp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Penicillium_roqueforti Penicillium roqueforti]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DGP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DGP FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Aristolochene_synthase Aristolochene synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.3.9 4.2.3.9] </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]] 2.8&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FOF:(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-ol'>FOF</scene>, <scene name='pdbligand=FOH:FARNESOL'>FOH</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=1dgp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dgp OCA], [https://pdbe.org/1dgp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dgp RCSB], [https://www.ebi.ac.uk/pdbsum/1dgp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dgp ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1di1|1DI1]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dgp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dgp OCA], [http://www.ebi.ac.uk/pdbsum/1dgp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dgp RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/PRX2_PENRO PRX2_PENRO] Aristolochene synthase; part of the gene cluster that mediates the biosynthesis of PR-toxin, a bicyclic sesquiterpene belonging to the eremophilane class and acting as a mycotoxin (PubMed:24239699, PubMed:27921136). The first step of the pathway is catalyzed by the aristolochene synthase which performs the cyclization of trans,trans-farnesyl diphosphate (FPP) to the bicyclic sesquiterpene aristolochene (PubMed:8440737, PubMed:15186158, PubMed:24239699). Following the formation of aristolochene, the non-oxygenated aristolochene is converted to the trioxygenated intermediate eremofortin B, via 7-epi-neopetasone (PubMed:24239699, PubMed:26274339). This conversion appears to involve three enzymes, a hydroxysterol oxidase-like enzyme, the quinone-oxidase prx3 that forms the quinone-type-structure in the bicyclic nucleus of aristolochene with the C8-oxo group and the C-3 hydroxyl group, and the P450 monooxygenase ORF6 that introduces the epoxide at the double bond between carbons 1 and 2 (PubMed:24239699, PubMed:27921136). No monoxy or dioxy-intermediates have been reported to be released to the broth, so these three early oxidative reactions may be coupled together (PubMed:24239699). Eremofortin B is further oxidized by another P450 monooxygenase, that introduces a second epoxide between carbons 7 and 11 prior to acetylation to eremofortin A by the acetyltransferase ORF8 (PubMed:16345540, PubMed:24239699, PubMed:27921136). The second epoxidation may be performed by a second P450 monooxygenase (PubMed:24239699). After the acetylation step, the conversion of eremofortin A to eremofortin C and then to PR-toxin requires only two enzymes (PubMed:24239699). First the conversion of eremofortin A to eremofortin C proceeds by oxidation of the side chain of the molecule at C-12 and is catalyzed by the short-chain oxidoreductase prx1 (PubMed:16345540, PubMed:24239699). The cytochrome P450 monooxygenase ORF5 also plays a role in this step (PubMed:27921136). The primary alcohol formed at C-12 is finally oxidized by the short-chain alcohol dehydrogenase prx4 that forms PR-toxin (PubMed:16345540, PubMed:24239699).<ref>PMID:15186158</ref> <ref>PMID:16345540</ref> <ref>PMID:24239699</ref> <ref>PMID:26274339</ref> <ref>PMID:27921136</ref> <ref>PMID:8440737</ref>
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== Evolutionary Conservation ==
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'''ARISTOLOCHENE SYNTHASE FARNESOL COMPLEX'''
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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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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dg/1dgp_consurf.spt"</scriptWhenChecked>
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The 2.5-A resolution crystal structure of recombinant aristolochene synthase from the blue cheese mold, Penicillium roqueforti, is the first of a fungal terpenoid cyclase. The structure of the enzyme reveals active site features that participate in the cyclization of the universal sesquiterpene cyclase substrate, farnesyl diphosphate, to form the bicyclic hydrocarbon aristolochene. Metal-triggered carbocation formation initiates the cyclization cascade, which proceeds through multiple complex intermediates to yield one exclusive structural and stereochemical isomer of aristolochene. Structural homology of this fungal cyclase with plant and bacterial terpenoid cyclases, despite minimal amino acid sequence identity, suggests divergence from a common, primordial ancestor in the evolution of terpene biosynthesis.
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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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==About this Structure==
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</jmolCheckbox>
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1DGP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Penicillium_roqueforti Penicillium roqueforti]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DGP OCA].
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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=1dgp ConSurf].
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<div style="clear:both"></div>
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==Reference==
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== References ==
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Crystal structure determination of aristolochene synthase from the blue cheese mold, Penicillium roqueforti., Caruthers JM, Kang I, Rynkiewicz MJ, Cane DE, Christianson DW, J Biol Chem. 2000 Aug 18;275(33):25533-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10825154 10825154]
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<references/>
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[[Category: Aristolochene synthase]]
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Penicillium roqueforti]]
[[Category: Penicillium roqueforti]]
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[[Category: Single protein]]
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[[Category: Cane DE]]
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[[Category: Cane, D E.]]
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[[Category: Caruthers JM]]
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[[Category: Caruthers, J M.]]
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[[Category: Christianson DW]]
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[[Category: Christianson, D W.]]
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[[Category: Kang I]]
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[[Category: Kang, I.]]
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[[Category: isoprenoid biosynthesis]]
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[[Category: sesquiterpene cyclase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:41:25 2008''
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Current revision

ARISTOLOCHENE SYNTHASE FARNESOL COMPLEX

PDB ID 1dgp

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