6sm6: Difference between revisions
New page: '''Unreleased structure''' The entry 6sm6 is ON HOLD until Paper Publication Authors: Description: Category: Unreleased Structures |
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==AntF (holo): type II PKS acyl-carrier protein== | |||
<StructureSection load='6sm6' size='340' side='right'caption='[[6sm6]], [[Resolution|resolution]] 2.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6sm6]] 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=6SM6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SM6 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]] 2.4Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4HH:O-[(S)-HYDROXY{[(3R)-3-HYDROXY-2,2-DIMETHYL-4-OXO-4-({3-OXO-3-[(2-SULFANYLETHYL)AMINO]PROPYL}AMINO)BUTYL]OXY}PHOSPHORYL]-L-SERINE'>4HH</scene></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=6sm6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sm6 OCA], [https://pdbe.org/6sm6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6sm6 RCSB], [https://www.ebi.ac.uk/pdbsum/6sm6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6sm6 ProSAT]</span></td></tr> | |||
</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> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6sm6" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Acyl carrier protein 3D structures|Acyl carrier protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Photorhabdus luminescens]] | |||
[[Category: Bode H]] | |||
[[Category: Braeuer A]] | |||
[[Category: Grammbitter GLC]] | |||
[[Category: Groll M]] | |||
[[Category: Kaila VRI]] | |||
[[Category: Ruehl M]] | |||
[[Category: Schmalhofer M]] | |||
[[Category: Zhou Q]] | |||
Latest revision as of 15:44, 24 January 2024
AntF (holo): type II PKS acyl-carrier proteinAntF (holo): 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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