6ad3: Difference between revisions
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==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]] | |||
Latest revision as of 10:31, 27 March 2024
Structural characterization of the condensation domain from Monacolin K polyketide synthase MokA
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