6H6X
Structure of an evolved dimeric form of the UbiD-class enzyme HmfF from Pelotomaculum thermopropionicum in complex with prFMN
Summary for 6H6X
| Entry DOI | 10.2210/pdb6h6x/pdb |
| Descriptor | 3-polyprenyl-4-hydroxybenzoate decarboxylase and related decarboxylases, POTASSIUM ION, MANGANESE (II) ION, ... (6 entities in total) |
| Functional Keywords | prfmn, decarboxylation, thermophilic, ubid, hmff, flavoprotein |
| Biological source | Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI) |
| Total number of polymer chains | 2 |
| Total formula weight | 99081.93 |
| Authors | Payne, K.A.P.,Leys, D. (deposition date: 2018-07-30, release date: 2019-02-27, Last modification date: 2024-01-17) |
| Primary citation | Payne, K.A.P.,Marshall, S.A.,Fisher, K.,Cliff, M.J.,Cannas, D.M.,Yan, C.,Heyes, D.J.,Parker, D.A.,Larrosa, I.,Leys, D. Enzymatic Carboxylation of 2-Furoic Acid Yields 2,5-Furandicarboxylic Acid (FDCA). Acs Catalysis, 9:2854-2865, 2019 Cited by PubMed Abstract: The biological production of FDCA is of considerable value as a potential replacement for petrochemical-derived monomers such as terephthalate, used in polyethylene terephthalate (PET) plastics. HmfF belongs to an uncharacterized branch of the prenylated flavin (prFMN) dependent UbiD family of reversible (de)carboxylases and is proposed to convert 2,5-furandicarboxylic acid (FDCA) to furoic acid in vivo. We present a detailed characterization of HmfF and demonstrate that HmfF can catalyze furoic acid carboxylation at elevated CO levels in vitro. We report the crystal structure of a thermophilic HmfF from , revealing that the active site located above the prFMN cofactor contains a furoic acid/FDCA binding site composed of residues H296-R304-R331 specific to the HmfF branch of UbiD enzymes. Variants of the latter are compromised in activity, while H296N alters the substrate preference to pyrrole compounds. Solution studies and crystal structure determination of an engineered dimeric form of the enzyme revealed an unexpected key role for a UbiD family wide conserved Leu residue in activity. The structural insights into substrate and cofactor binding provide a template for further exploitation of HmfF in the production of FDCA plastic precursors and improve our understanding of catalysis by members of the UbiD enzyme family. PubMed: 31057985DOI: 10.1021/acscatal.8b04862 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.25 Å) |
Structure validation
Download full validation report
