7abo
From Proteopedia
(Difference between revisions)
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==Structure of the N318H variant of the reversible pyrrole-2-carboxylic acid decarboxylase PA0254/HudA in complex with FMN== | ==Structure of the N318H variant of the reversible pyrrole-2-carboxylic acid decarboxylase PA0254/HudA in complex with FMN== | ||
| - | <StructureSection load='7abo' size='340' side='right'caption='[[7abo]]' scene=''> | + | <StructureSection load='7abo' size='340' side='right'caption='[[7abo]], [[Resolution|resolution]] 1.95Å' 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=7ABO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ABO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7abo]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ABO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ABO FirstGlance]. <br> |
| - | </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=7abo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7abo OCA], [https://pdbe.org/7abo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7abo RCSB], [https://www.ebi.ac.uk/pdbsum/7abo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7abo ProSAT]</span></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]] 1.95Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=7abo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7abo OCA], [https://pdbe.org/7abo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7abo RCSB], [https://www.ebi.ac.uk/pdbsum/7abo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7abo ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/FDC_PSEAE FDC_PSEAE] Catalyzes the reversible decarboxylation of aromatic carboxylic acids (Probable). Attenuates the virulence of P.aeruginosa in a Drosophila model when overexpressed (PubMed:18591226).[HAMAP-Rule:MF_01983]<ref>PMID:18591226</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The UbiD family of reversible (de)carboxylases depends on the recently discovered prenylated-FMN (prFMN) cofactor for activity. The model enzyme ferulic acid decarboxylase (Fdc1) decarboxylates unsaturated aliphatic acids via a reversible 1,3-cycloaddition process. Protein engineering has extended the Fdc1 substrate range to include (hetero)aromatic acids, although catalytic rates remain poor. This raises the question how efficient decarboxylation of (hetero)aromatic acids is achieved by other UbiD family members. Here, we show that the Pseudomonas aeruginosa virulence attenuation factor PA0254/HudA is a pyrrole-2-carboxylic acid decarboxylase. The crystal structure of the enzyme in the presence of the reversible inhibitor imidazole reveals a covalent prFMN-imidazole adduct is formed. Substrate screening reveals HudA and selected active site variants can accept a modest range of heteroaromatic compounds, including thiophene-2-carboxylic acid. Together with computational studies, our data suggests prFMN covalent catalysis occurs via electrophilic aromatic substitution and links HudA activity with the inhibitory effects of pyrrole-2-carboxylic acid on P. aeruginosa quorum sensing. | ||
| + | |||
| + | Structure and Mechanism of Pseudomonas aeruginosa PA0254/HudA, a prFMN-Dependent Pyrrole-2-carboxylic Acid Decarboxylase Linked to Virulence.,Payne KAP, Marshall SA, Fisher K, Rigby SEJ, Cliff MJ, Spiess R, Cannas DM, Larrosa I, Hay S, Leys D ACS Catal. 2021 Mar 5;11(5):2865-2878. doi: 10.1021/acscatal.0c05042. Epub 2021, Feb 17. PMID:33763291<ref>PMID:33763291</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7abo" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| + | [[Category: Pseudomonas aeruginosa]] | ||
[[Category: Leys D]] | [[Category: Leys D]] | ||
[[Category: Marshall SA]] | [[Category: Marshall SA]] | ||
Current revision
Structure of the N318H variant of the reversible pyrrole-2-carboxylic acid decarboxylase PA0254/HudA in complex with FMN
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