8cg6

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Current revision (06:42, 3 July 2025) (edit) (undo)
 
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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=8cg6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8cg6 OCA], [https://pdbe.org/8cg6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8cg6 RCSB], [https://www.ebi.ac.uk/pdbsum/8cg6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8cg6 ProSAT]</span></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=8cg6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8cg6 OCA], [https://pdbe.org/8cg6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8cg6 RCSB], [https://www.ebi.ac.uk/pdbsum/8cg6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8cg6 ProSAT]</span></td></tr>
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== Function ==
 
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[https://www.uniprot.org/uniprot/CTB1_CERNC CTB1_CERNC] Polyketide synthase; part of the gene cluster that mediates the biosynthesis of cercosporin, a light-activated, non-host-selective toxin (PubMed:12937958, PubMed:15915645, PubMed:26938470, PubMed:29610486). The perylenequinone chromophore of cercosporin absorbs light energy to attain an electronically-activated triplet state and produces active oxygen species such as the hydroxyl radical, superoxide, hydrogen peroxide or singlet oxygen upon reaction with oxygen molecules (PubMed:11701851). These reactive oxygen species cause damage to various cellular components including lipids, proteins and nucleic acids (PubMed:11701851). The first step of cercosporin biosynthesis is performed by the polyketide synthase CTB1 which catalyzes the formation of nor-toralactone (PubMed:23108075, PubMed:26938470, PubMed:29610486). The starter unit acyltransferase (SAT) domain of CTB1 initiates polyketide extension by the selective utilization of acetyl-CoA, which is elongated to the heptaketide in the beta-ketoacyl synthase (KS) domain by successive condensations with six malonyl units introduced by the malonyl acyltransferase (MAT) domain. The product template (PT) domain catalyzes C4-C9 and C2-C11 aldol cyclizations and dehydrations to a trihydroxynaphthalene, which is thought to be delivered to the thioesterase (TE) domain for product release (PubMed:23108075, PubMed:29610486). The bifunctional enzyme CTB3 then methylates nor-toralactone to toralactone before conducting an unusual oxidative aromatic ring opening (PubMed:17074519, PubMed:26938470). The O-methyltransferase CTB2 further methylates the nascent OH-6 of the CBT3 product, blocking further oxidation at this site before the reductase CTB6 reduces the 2-oxopropyl ketone at position C7, giving naphthalene (PubMed:17660442, PubMed:26938470). The FAD-dependent monooxygenase CTB5 in concert with the multicopper oxidase CTB12 are responsible for homodimerization of naphthalene with CTB7 installing the dioxepine moiety, finally producing cercosporin (PubMed:17660442, PubMed:30809363, PubMed:26938470). The fasciclin domain-containing protein CTB11 might act with CTB5 and CTB12 whereas the roles of CTB9 and CTB10 have still to be elucidated (By similarity).[UniProtKB:Q0UHZ9]<ref>PMID:12937958</ref> <ref>PMID:15915645</ref> <ref>PMID:17074519</ref> <ref>PMID:17660442</ref> <ref>PMID:23108075</ref> <ref>PMID:26938470</ref> <ref>PMID:29610486</ref> <ref>PMID:30809363</ref> <ref>PMID:11701851</ref>
 
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== References ==
 
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<references/>
 
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Current revision

The ACP crosslinked to the SAT of the cercosporin fungal non-reducing polyketide synthase (NR-PKS) CTB1 (ACP:SAT-KS-MAT)

PDB ID 8cg6

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