5m3k
From Proteopedia
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<StructureSection load='5m3k' size='340' side='right' caption='[[5m3k]], [[Resolution|resolution]] 2.83Å' scene=''> | <StructureSection load='5m3k' size='340' side='right' caption='[[5m3k]], [[Resolution|resolution]] 2.83Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5m3k]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M3K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5M3K FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5m3k]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_fluorescens_liquefaciens"_flugge_1886 "bacillus fluorescens liquefaciens" flugge 1886] and [http://en.wikipedia.org/wiki/Psef5 Psef5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M3K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5M3K FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SCY:S-ACETYL-CYSTEINE'>SCY</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SCY:S-ACETYL-CYSTEINE'>SCY</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">phlA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=294 "Bacillus fluorescens liquefaciens" Flugge 1886]), phlB, PFL_5956 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=220664 PSEF5]), phlC, PFL_5955 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=220664 PSEF5])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5m3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m3k OCA], [http://pdbe.org/5m3k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5m3k RCSB], [http://www.ebi.ac.uk/pdbsum/5m3k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5m3k ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5m3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m3k OCA], [http://pdbe.org/5m3k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5m3k RCSB], [http://www.ebi.ac.uk/pdbsum/5m3k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5m3k ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | C-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. | ||
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| + | 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<ref>PMID:30318713</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5m3k" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Bacillus fluorescens liquefaciens flugge 1886]] | ||
| + | [[Category: Psef5]] | ||
[[Category: Gruber, K]] | [[Category: Gruber, K]] | ||
[[Category: Kroutil, W]] | [[Category: Kroutil, W]] | ||
Revision as of 07:06, 31 October 2018
A multi-component acyltransferase PhlABC from Pseudomonas protegens
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