5mg5: Difference between revisions
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==A multi-component acyltransferase PhlABC from Pseudomonas protegens soaked with the monoacetylphloroglucinol (MAPG)== | ==A multi-component acyltransferase PhlABC from Pseudomonas protegens soaked with the monoacetylphloroglucinol (MAPG)== | ||
<StructureSection load='5mg5' size='340' side='right' caption='[[5mg5]], [[Resolution|resolution]] 3.44Å' scene=''> | <StructureSection load='5mg5' size='340' side='right'caption='[[5mg5]], [[Resolution|resolution]] 3.44Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5mg5]] is a 24 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5mg5]] is a 24 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_protegens Pseudomonas protegens] and [https://en.wikipedia.org/wiki/Pseudomonas_protegens_Pf-5 Pseudomonas protegens Pf-5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MG5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MG5 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.44Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=13X:BENZENE-1,3,5-TRIOL'>13X</scene>, <scene name='pdbligand=SCY:S-ACETYL-CYSTEINE'>SCY</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=5mg5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mg5 OCA], [https://pdbe.org/5mg5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mg5 RCSB], [https://www.ebi.ac.uk/pdbsum/5mg5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mg5 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q4K420_PSEF5 Q4K420_PSEF5] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Pseudomonas protegens]] | ||
[[Category: Gruber | [[Category: Pseudomonas protegens Pf-5]] | ||
[[Category: Kroutil | [[Category: Gruber K]] | ||
[[Category: Pavkov-Keller | [[Category: Kroutil W]] | ||
[[Category: Schmidt | [[Category: Pavkov-Keller T]] | ||
[[Category: Schmidt NG]] | |||
Latest revision as of 21:42, 1 November 2023
A multi-component acyltransferase PhlABC from Pseudomonas protegens soaked with the monoacetylphloroglucinol (MAPG)A multi-component acyltransferase PhlABC from Pseudomonas protegens soaked with the monoacetylphloroglucinol (MAPG)
Structural highlights
FunctionPublication Abstract from PubMedC-C bond forming reactions are key transformations to set up the carbon framework of organic molecules. In this context, the Friedel-Crafts acylation is commonly used for the synthesis of aryl ketones, which are common motifs in many fine chemicals and natural products. A bacterial multi-component acyltransferase from Pseudomonas protegens (PpATase) catalyzes such a Friedel-Crafts C-acylation of phenolic substrates in aqueous solution reaching up to >99% conversion without the need of CoA-activated reagents. We determined x-ray crystal structures of the native and ligand-bound complex. This multimeric enzyme consists of three subunits - PhlA, PhlB and PhlC which are arranged in a Phl(A2C2)2B4 composition. The structure of a reaction intermediate obtained from crystals soaked with the natural substrate monoacetylphloroglucinol together with site-directed mutagenesis studies revealed that only residues from the PhlC subunits are involved in the acyl transfer reaction, with Cys88 very likely playing a significant role during catalysis. These structural and mechanistic insights form the basis of further enzyme engineering efforts towards enhancing the substrate scope of this enzyme. Structure and catalytic mechanism of a bacterial Friedel-Crafts acylase.,Pavkov-Keller T, Schmidt NG, Zadlo-Dobrowolska A, Kroutil W, Gruber K Chembiochem. 2018 Oct 14. doi: 10.1002/cbic.201800462. PMID:30318713[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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