7ABN
Structure of the reversible pyrrole-2-carboxylic acid decarboxylase PA0254/HudA
Summary for 7ABN
| Entry DOI | 10.2210/pdb7abn/pdb |
| Descriptor | UbiD-like decarboxylase, MANGANESE (II) ION, POTASSIUM ION, ... (6 entities in total) |
| Functional Keywords | prfmn, decarboxylase, ubid, pyrrole, pyrrole-2-carboxylic acid, ligase |
| Biological source | Pseudomonas aeruginosa |
| Total number of polymer chains | 4 |
| Total formula weight | 221013.74 |
| Authors | Leys, D. (deposition date: 2020-09-08, release date: 2021-04-07, Last modification date: 2024-01-31) |
| Primary citation | Payne, K.A.P.,Marshall, S.A.,Fisher, K.,Rigby, S.E.J.,Cliff, M.J.,Spiess, R.,Cannas, D.M.,Larrosa, I.,Hay, S.,Leys, D. Structure and Mechanism of Pseudomonas aeruginosa PA0254/HudA, a prFMN-Dependent Pyrrole-2-carboxylic Acid Decarboxylase Linked to Virulence. Acs Catalysis, 11:2865-2878, 2021 Cited by PubMed Abstract: 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 virulence attenuation factor PA0254HudA is a pyrrole-2-carboxylic acid decarboxylase. The crystal structure of the enzyme in the presence of the reversible inhibitor imidazole reveals a covalent prFMNimidazole 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 quorum sensing. PubMed: 33763291DOI: 10.1021/acscatal.0c05042 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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