1di1: Difference between revisions
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New page: left|200px<br /><applet load="1di1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1di1, resolution 2.5Å" /> '''CRYSTAL STRUCTURE OF ... |
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== | ==CRYSTAL STRUCTURE OF ARISTOLOCHENE SYNTHASE FROM PENICILLIUM ROQUEFORTI== | ||
<StructureSection load='1di1' size='340' side='right'caption='[[1di1]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
== | <table><tr><td colspan='2'>[[1di1]] 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=1DI1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DI1 FirstGlance]. <br> | ||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</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=1di1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1di1 OCA], [https://pdbe.org/1di1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1di1 RCSB], [https://www.ebi.ac.uk/pdbsum/1di1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1di1 ProSAT]</span></td></tr> | |||
== | </table> | ||
== Function == | |||
[[Category: | [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> | ||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/di/1di1_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=1di1 ConSurf]. | |||
<div style="clear:both"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Penicillium roqueforti]] | [[Category: Penicillium roqueforti]] | ||
[[Category: Cane DE]] | |||
[[Category: Cane | [[Category: Caruthers JM]] | ||
[[Category: Caruthers | [[Category: Christianson DW]] | ||
[[Category: Christianson | [[Category: Kang I]] | ||
[[Category: Kang | [[Category: Rynkiewicz MJ]] | ||
[[Category: Rynkiewicz | |||
Latest revision as of 06:53, 7 February 2024
CRYSTAL STRUCTURE OF ARISTOLOCHENE SYNTHASE FROM PENICILLIUM ROQUEFORTI
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