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6ad3
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 6ad3 is ON HOLD Authors: Wang, L., Zheng, J. Description: Structural characterization of the condensation domain from Monacolin K polyketide syntha...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Structural characterization of the condensation domain from Monacolin K polyketide synthase MokA== | |
| - | + | <StructureSection load='6ad3' size='340' side='right'caption='[[6ad3]], [[Resolution|resolution]] 1.79Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[6ad3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Monascus_pilosus Monascus pilosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AD3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6AD3 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]] 1.79Å</td></tr> | |
| - | [[Category: | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6ad3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ad3 OCA], [https://pdbe.org/6ad3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ad3 RCSB], [https://www.ebi.ac.uk/pdbsum/6ad3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ad3 ProSAT]</span></td></tr> |
| - | [[Category: | + | </table> |
| - | [[Category: Wang | + | == Function == |
| + | [https://www.uniprot.org/uniprot/MOKA_MONPI MOKA_MONPI] Nonaketide synthase; part of the gene cluster that mediates the biosynthesis of monakolin K, also known as lovastatin, and which acts as a potent competitive inhibitor of HMG-CoA reductase (PubMed:18578535). Monakolin K biosynthesis is performed in two stages (PubMed:19693441). The first stage is catalyzed by the nonaketide synthase mokA, which belongs to type I polyketide synthases and catalyzes the iterative nine-step formation of the polyketide (PubMed:18578535, PubMed:19693441). This PKS stage is completed by the action of dehydrogenase mokE, which catalyzes the NADPH-dependent reduction of the unsaturated tetra-, penta- and heptaketide intermediates that arise during the mokA-mediated biosynthesis of the nonaketide chain and leads to dihydromonacolin L (PubMed:19693441). Covalently bound dihydromonacolin L is released from mokA by the mokD esterase (By similarity). Conversion of dihydromonacolin L into monacolin L and then monacolin J is subsequently performed with the participation of molecular oxygen and P450 monoogygenase mokC (PubMed:19693441). Finally, mokF performs the conversion of monacoline J to monacoline K through the addition of the side-chain diketide moiety (2R)-2-methylbutanoate produced by the diketide synthase mokB (PubMed:19693441).[UniProtKB:Q0C8M2][UniProtKB:Q9Y8A5]<ref>PMID:18578535</ref> <ref>PMID:19693441</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Monascus pilosus]] | ||
| + | [[Category: Wang L]] | ||
| + | [[Category: Zheng J]] | ||
Current revision
Structural characterization of the condensation domain from Monacolin K polyketide synthase MokA
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