6sm4: Difference between revisions
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==AntF (apo): type II PKS acyl-carrier protein== | ==AntF (apo): type II PKS acyl-carrier protein== | ||
<StructureSection load='6sm4' size='340' side='right'caption='[[6sm4]]' scene=''> | <StructureSection load='6sm4' size='340' side='right'caption='[[6sm4]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SM4 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6sm4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Photorhabdus_luminescens Photorhabdus luminescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SM4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SM4 FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85Å</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=6sm4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sm4 OCA], [https://pdbe.org/6sm4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6sm4 RCSB], [https://www.ebi.ac.uk/pdbsum/6sm4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6sm4 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A2S8QL96_PHOLU A0A2S8QL96_PHOLU] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Type II polyketide synthases (PKSs) are multi-enzyme complexes that produce secondary metabolites of medical relevance. Chemical backbones of such polyketides are produced by minimal PKS systems that consist of a malonyl transacylase, an acyl carrier protein and an alpha/beta heterodimeric ketosynthase. Here, we present X-ray structures of all ternary complexes that constitute the minimal PKS system for anthraquinone biosynthesis in Photorhabdus luminescens. In addition, we characterize this invariable core using molecular simulations, mutagenesis experiments and functional assays. We show that malonylation of the acyl carrier protein is accompanied by major structural rearrangements in the transacylase. Principles of an ongoing chain elongation are derived from the ternary complex with a hexaketide covalently linking the heterodimeric ketosynthase with the acyl carrier protein. Our results for the minimal PKS system provide mechanistic understanding of PKSs and a fundamental basis for engineering PKS pathways for future applications. | |||
Structural snapshots of the minimal PKS system responsible for octaketide biosynthesis.,Brauer A, Zhou Q, Grammbitter GLC, Schmalhofer M, Ruhl M, Kaila VRI, Bode HB, Groll M Nat Chem. 2020 Aug;12(8):755-763. doi: 10.1038/s41557-020-0491-7. Epub 2020 Jul, 6. PMID:32632186<ref>PMID:32632186</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6sm4" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Acyl carrier protein 3D structures|Acyl carrier protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Photorhabdus luminescens]] | |||
[[Category: Bode H]] | [[Category: Bode H]] | ||
[[Category: Braeuer A]] | [[Category: Braeuer A]] | ||
Latest revision as of 15:44, 24 January 2024
AntF (apo): type II PKS acyl-carrier proteinAntF (apo): type II PKS acyl-carrier protein
Structural highlights
FunctionPublication Abstract from PubMedType II polyketide synthases (PKSs) are multi-enzyme complexes that produce secondary metabolites of medical relevance. Chemical backbones of such polyketides are produced by minimal PKS systems that consist of a malonyl transacylase, an acyl carrier protein and an alpha/beta heterodimeric ketosynthase. Here, we present X-ray structures of all ternary complexes that constitute the minimal PKS system for anthraquinone biosynthesis in Photorhabdus luminescens. In addition, we characterize this invariable core using molecular simulations, mutagenesis experiments and functional assays. We show that malonylation of the acyl carrier protein is accompanied by major structural rearrangements in the transacylase. Principles of an ongoing chain elongation are derived from the ternary complex with a hexaketide covalently linking the heterodimeric ketosynthase with the acyl carrier protein. Our results for the minimal PKS system provide mechanistic understanding of PKSs and a fundamental basis for engineering PKS pathways for future applications. Structural snapshots of the minimal PKS system responsible for octaketide biosynthesis.,Brauer A, Zhou Q, Grammbitter GLC, Schmalhofer M, Ruhl M, Kaila VRI, Bode HB, Groll M Nat Chem. 2020 Aug;12(8):755-763. doi: 10.1038/s41557-020-0491-7. Epub 2020 Jul, 6. PMID:32632186[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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