5wqh

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Current revision (16:51, 8 November 2023) (edit) (undo)
 
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<StructureSection load='5wqh' size='340' side='right'caption='[[5wqh]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='5wqh' size='340' side='right'caption='[[5wqh]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5wqh]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WQH OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5WQH FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5wqh]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_terreus_NIH2624 Aspergillus terreus NIH2624]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WQH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WQH FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=7WU:methyl+(2S,4aR,4bS,5S,6aS,10aS,10bS,12aS)-2,4b,7,7,10a,12,12a-heptamethyl-5-oxidanyl-1,4,6,8-tetrakis(oxidanylidene)-4a,5,6a,9,10,10b-hexahydronaphtho[1,2-h]isochromene-2-carboxylate'>7WU</scene>, <scene name='pdbligand=7WX:methyl+(5S,7S,8S,9S,10S,13R,14R,16S)-4,4,8,10,12,13,16-heptamethyl-7,16-bis(oxidanyl)-3,6,15,17-tetrakis(oxidanylidene)-2,5,7,9-tetrahydro-1H-cyclopenta[a]phenanthrene-14-carboxylate'>7WX</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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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]] 2.102&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5wqf|5wqf]], [[5wqg|5wqg]], [[5wqi|5wqi]]</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=7WU:methyl+(2S,4aR,4bS,5S,6aS,10aS,10bS,12aS)-2,4b,7,7,10a,12,12a-heptamethyl-5-oxidanyl-1,4,6,8-tetrakis(oxidanylidene)-4a,5,6a,9,10,10b-hexahydronaphtho[1,2-h]isochromene-2-carboxylate'>7WU</scene>, <scene name='pdbligand=7WX:methyl+(5S,7S,8S,9S,10S,13R,14R,16S)-4,4,8,10,12,13,16-heptamethyl-7,16-bis(oxidanyl)-3,6,15,17-tetrakis(oxidanylidene)-2,5,7,9-tetrahydro-1H-cyclopenta[a]phenanthrene-14-carboxylate'>7WX</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5wqh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wqh OCA], [http://pdbe.org/5wqh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wqh RCSB], [http://www.ebi.ac.uk/pdbsum/5wqh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wqh ProSAT]</span></td></tr>
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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=5wqh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wqh OCA], [https://pdbe.org/5wqh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wqh RCSB], [https://www.ebi.ac.uk/pdbsum/5wqh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wqh ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/TRT14_ASPTN TRT14_ASPTN]] Isomerase; part of the gene cluster that mediates the biosynthesis of terretonin, a fungal meroterpenoid that acts as a mycotoxin (PubMed:22549923, PubMed:23116177, PubMed:25671343). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase trt4 (PubMed:22549923, PubMed:23116177). DMOA is then prenylated into farnesyl-DMOA by the polyprenyl transferase trt2 (PubMed:22549923, PubMed:22782788, PubMed:23116177). Methylation by the methyltransferase trt5 then leads to farnesyl-DMOA methyl ester which is further subject to epoxidation by the FAD-dependent monooxygenase trt8 to yield epoxyfarnesyl-DMOA methyl ester (PubMed:22549923, PubMed:22782788, PubMed:23116177). Cyclization of epoxyfarnesyl-DMOA methyl ester by the terpene cyclase trt1 leads to a tetracycle intermediate which is in turn converted to preterretonin (PubMed:22549923, PubMed:22782788, PubMed:23116177). Dehydrogenase trt9 comes next to transform preterretonin to preterrenoid (PubMed:22549923, PubMed:23116177). The FAD-dependent monooxygenase trt3 is then required for the C-hydroxylation at C16 of preterrenoid to yield terrenoid (PubMed:22549923, PubMed:23116177). The cytochrome P450 trt6 catalyzes three successive oxidations to transform terrenoid into an unstable intermediate, which then undergoes the D-ring expansion and unusual rearrangement of the methoxy group to afford the core skeleton of terretonin (PubMed:25671343). This unprecedented rearrangement is catalyzed by the isomerase trt14 (PubMed:25671343). Finally, the nonheme iron-dependent dioxygenase trt7 accomplishes the last two oxidation reactions steps to complete the biosynthesis of terretonin (PubMed:25671343). Terretonin C is produced via spontaneous decarboxylation of the terretonin precursor (PubMed:23116177). Another shunt product of the terretonin biosynthesis is dihydrofarnesyl-DMOA, derived from epoxyfarnesyl-DMOA through hydrolysis of the epoxide (PubMed:22549923, PubMed:22782788, PubMed:23116177).<ref>PMID:22549923</ref> <ref>PMID:22782788</ref> <ref>PMID:23116177</ref> <ref>PMID:25671343</ref>
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[https://www.uniprot.org/uniprot/TRT14_ASPTN TRT14_ASPTN] Isomerase; part of the gene cluster that mediates the biosynthesis of terretonin, a fungal meroterpenoid that acts as a mycotoxin (PubMed:22549923, PubMed:23116177, PubMed:25671343). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase trt4 (PubMed:22549923, PubMed:23116177). DMOA is then prenylated into farnesyl-DMOA by the polyprenyl transferase trt2 (PubMed:22549923, PubMed:22782788, PubMed:23116177). Methylation by the methyltransferase trt5 then leads to farnesyl-DMOA methyl ester which is further subject to epoxidation by the FAD-dependent monooxygenase trt8 to yield epoxyfarnesyl-DMOA methyl ester (PubMed:22549923, PubMed:22782788, PubMed:23116177). Cyclization of epoxyfarnesyl-DMOA methyl ester by the terpene cyclase trt1 leads to a tetracycle intermediate which is in turn converted to preterretonin (PubMed:22549923, PubMed:22782788, PubMed:23116177). Dehydrogenase trt9 comes next to transform preterretonin to preterrenoid (PubMed:22549923, PubMed:23116177). The FAD-dependent monooxygenase trt3 is then required for the C-hydroxylation at C16 of preterrenoid to yield terrenoid (PubMed:22549923, PubMed:23116177). The cytochrome P450 trt6 catalyzes three successive oxidations to transform terrenoid into an unstable intermediate, which then undergoes the D-ring expansion and unusual rearrangement of the methoxy group to afford the core skeleton of terretonin (PubMed:25671343). This unprecedented rearrangement is catalyzed by the isomerase trt14 (PubMed:25671343). Finally, the nonheme iron-dependent dioxygenase trt7 accomplishes the last two oxidation reactions steps to complete the biosynthesis of terretonin (PubMed:25671343). Terretonin C is produced via spontaneous decarboxylation of the terretonin precursor (PubMed:23116177). Another shunt product of the terretonin biosynthesis is dihydrofarnesyl-DMOA, derived from epoxyfarnesyl-DMOA through hydrolysis of the epoxide (PubMed:22549923, PubMed:22782788, PubMed:23116177).<ref>PMID:22549923</ref> <ref>PMID:22782788</ref> <ref>PMID:23116177</ref> <ref>PMID:25671343</ref>
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Aspergillus terreus NIH2624]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Abe, I]]
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[[Category: Abe I]]
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[[Category: Matsuda, Y]]
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[[Category: Matsuda Y]]
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[[Category: Mori, T]]
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[[Category: Mori T]]
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[[Category: Isomerase]]
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[[Category: Meroterpenoid]]
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[[Category: Terretonin]]
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Current revision

Structure of fungal meroterpenoid isomerase Trt14 complexed with substrate analog and endo-terretonin D

PDB ID 5wqh

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