6h6v

Structure of the UbiD-class enzyme HmfF from Pelotomaculum thermopropionicum in complex with FMN

spinqualitylabelsall models 6h6v, resolution 2.66Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6h6v is a 6 chain structure with sequence from Pelotomaculum thermopropionicum SI. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.66Å Ligands: CA, FMN, K, MN, MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A5D4Z9_PELTS Publication Abstract from PubMed 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 CO2 levels in vitro. We report the crystal structure of a thermophilic HmfF from Pelotomaculum thermopropionicum, 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. Enzymatic Carboxylation of 2-Furoic Acid Yields 2,5-Furandicarboxylic Acid (FDCA).,Payne KAP, Marshall SA, Fisher K, Cliff MJ, Cannas DM, Yan C, Heyes DJ, Parker DA, Larrosa I, Leys D ACS Catal. 2019 Apr 5;9(4):2854-2865. doi: 10.1021/acscatal.8b04862. Epub 2019, Feb 15. PMID:31057985 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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