8czc

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<StructureSection load='8czc' size='340' side='right'caption='[[8czc]], [[Resolution|resolution]] 2.86&Aring;' scene=''>
<StructureSection load='8czc' size='340' side='right'caption='[[8czc]], [[Resolution|resolution]] 2.86&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[8czc]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8CZC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8CZC FirstGlance]. <br>
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<table><tr><td colspan='2'>[[8czc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_venezuelae Streptomyces venezuelae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8CZC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8CZC FirstGlance]. <br>
</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=8czc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8czc OCA], [https://pdbe.org/8czc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8czc RCSB], [https://www.ebi.ac.uk/pdbsum/8czc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8czc ProSAT]</span></td></tr>
</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=8czc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8czc OCA], [https://pdbe.org/8czc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8czc RCSB], [https://www.ebi.ac.uk/pdbsum/8czc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8czc ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/PIKA1_STRVZ PIKA1_STRVZ]] Involved in the biosynthesis of 12- and 14-membered ring macrolactone antibiotics such as methymycin and neomethymycin, and pikromycin and narbomycin, respectively. Component of the pikromycin PKS which catalyzes the biosynthesis of both precursors 10-deoxymethynolide (12-membered ring macrolactone) and narbonolide (14-membered ring macrolactone) (PubMed:18512859, PubMed:19437523). Chain elongation through PikAI, PikAII and PikAIII followed by thioesterase catalyzed termination results in the production of 10-deoxymethynolide, while continued elongation through PikAIV, followed by thioesterase (TE) catalyzed cyclization results in the biosynthesis of the narbonolide.<ref>PMID:10421766</ref> <ref>PMID:18512859</ref> <ref>PMID:19437523</ref> <ref>PMID:19027305</ref>
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[[https://www.uniprot.org/uniprot/PIKA1_STRVZ PIKA1_STRVZ]] Involved in the biosynthesis of 12- and 14-membered ring macrolactone antibiotics such as methymycin and neomethymycin, and pikromycin and narbomycin, respectively. Component of the pikromycin PKS which catalyzes the biosynthesis of both precursors 10-deoxymethynolide (12-membered ring macrolactone) and narbonolide (14-membered ring macrolactone) (PubMed:18512859, PubMed:19437523). Chain elongation through PikAI, PikAII and PikAIII followed by thioesterase catalyzed termination results in the production of 10-deoxymethynolide, while continued elongation through PikAIV, followed by thioesterase (TE) catalyzed cyclization results in the biosynthesis of the narbonolide.<ref>PMID:10421766</ref> <ref>PMID:18512859</ref> <ref>PMID:19437523</ref> <ref>PMID:19027305</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The first domain of modular polyketide synthases (PKSs) is most commonly a ketosynthase (KS)-like enzyme, KS(Q), that primes polyketide synthesis. Unlike downstream KSs that fuse alpha-carboxyacyl groups to growing polyketide chains, it performs an extension-decoupled decarboxylation of these groups to generate primer units. When Pik127, a model triketide synthase constructed from modules of the pikromycin synthase, was studied by cryoelectron microscopy (cryo-EM), the dimeric didomain comprised of KS(Q) and the neighboring methylmalonyl-selective acyltransferase (AT) dominated the class averages and yielded structures at 2.5- and 2.8-A resolution, respectively. Comparisons with ketosynthases complexed with their substrates revealed the conformation of the (2S)-methylmalonyl-S-phosphopantetheinyl portion of KS(Q) and KS substrates prior to decarboxylation. Point mutants of Pik127 probed the roles of residues in the KS(Q) active site, while an AT-swapped version of Pik127 demonstrated that KS(Q) can also decarboxylate malonyl groups. Mechanisms for how KS(Q) and KS domains catalyze carbon-carbon chemistry are proposed.
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Priming enzymes from the pikromycin synthase reveal how assembly-line ketosynthases catalyze carbon-carbon chemistry.,Dickinson MS, Miyazawa T, McCool RS, Keatinge-Clay AT Structure. 2022 Jun 13. pii: S0969-2126(22)00230-1. doi:, 10.1016/j.str.2022.05.021. PMID:35738283<ref>PMID:35738283</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 8czc" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Dickinson, M S]]
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[[Category: Streptomyces venezuelae]]
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[[Category: Keatinge-Clay, A T]]
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[[Category: Dickinson MS]]
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[[Category: McCool, R S]]
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[[Category: Keatinge-Clay AT]]
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[[Category: Miyazawa, T]]
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[[Category: McCool RS]]
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[[Category: Acyltransferase]]
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[[Category: Miyazawa T]]
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[[Category: Biosynthetic protein]]
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[[Category: Methylmalonyl-specific]]
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[[Category: Polyketide synthase]]
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Revision as of 07:26, 8 September 2022

AT from first module of the pikromycin synthase

PDB ID 8czc

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