7r0x
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7r0x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Serratia Serratia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7R0X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7R0X FirstGlance]. <br> | <table><tr><td colspan='2'>[[7r0x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Serratia Serratia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7R0X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7R0X FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.83Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=7r0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7r0x OCA], [https://pdbe.org/7r0x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7r0x RCSB], [https://www.ebi.ac.uk/pdbsum/7r0x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7r0x ProSAT]</span></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=7r0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7r0x OCA], [https://pdbe.org/7r0x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7r0x RCSB], [https://www.ebi.ac.uk/pdbsum/7r0x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7r0x ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/A0A318P693_SERPL A0A318P693_SERPL] | |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| - | Thioesterases (TEs) are fundamentally important enzymes present in all bacteria and eukaryotes, where they have conserved functions in fatty acid biosynthesis and secondary metabolism. This work provides the first structural insights into a functionally distinct group of TEs that perform diverse acylations in polyketide and peptide biosynthesis (TE B s). Structural analysis of the oocydin (OocS) TE B domain facilitated identification and engineering of the active site to modulate acyl-group acceptance. In this way, we achieved higher reactivity using a structure-based approach, building a foundation for biocatalytic development of TE B -mediated O -acylation, a modification known to improve the bioactivity of oocydin-type polyketides. Lastly, the promiscuity of the OocS TE B motivated us to investigate, and ultimately provide evidence for, the production of longer chain branched oocydins in the native host Serratia plymuthica 4Rx13. This work frames the OocS TE B and homologs as invaluable synthetic biology tools for polyketide drug development. | + | Thioesterases (TEs) are fundamentally important enzymes present in all bacteria and eukaryotes, where they have conserved functions in fatty acid biosynthesis and secondary metabolism. This work provides the first structural insights into a functionally distinct group of TEs that perform diverse acylations in polyketide and peptide biosynthesis (TE(B) s). Structural analysis of the oocydin (OocS) TE(B) domain facilitated identification and engineering of the active site to modulate acyl-group acceptance. In this way, we achieved higher reactivity using a structure-based approach, building a foundation for biocatalytic development of TE(B) -mediated O-acylation, a modification known to improve the bioactivity of oocydin-type polyketides. Lastly, the promiscuity of the OocS TE(B) motivated us to investigate, and ultimately provide evidence for, the production of longer chain branched oocydins in the native host Serratia plymuthica 4Rx13. This work frames the OocS TE(B) and homologs as invaluable synthetic biology tools for polyketide drug development. |
| - | Structure of a | + | Structure of a Promiscuous Thioesterase Domain Responsible for Branching Acylation in Polyketide Biosynthesis.,Fraley AE, Dieterich CL, Mabesoone MFJ, Minas HA, Meoded RA, Hemmerling F, Piel J Angew Chem Int Ed Engl. 2022 Sep 26;61(39):e202206385. doi: , 10.1002/anie.202206385. Epub 2022 Aug 19. PMID:35903999<ref>PMID:35903999</ref> |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
Current revision
Structure of the branching thioesterase from oocydin biosynthesis
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