Title: Crystal structure of the Fusarium oxysporum tannase-like feruloyl esterase FaeC in complex with p-coumaric acid provides insight into ligand binding Ferousi C, Kosinas C, Nikolaivits E, Topakas E, Dimarogona M Ref: FEBS Letters, :, 2023 : PubMed
Feruloyl esterases (FAEs) hydrolyze the ester bonds between hydroxycinnamic acids and arabinose residues of plant cell walls and exhibit considerable diversity in terms of substrate specificity. Here, we report the crystal structure of an FAE from Fusarium oxysporum (FoFaeC) at 1.7 A resolution in complex with p-coumaric acid, which is the first ligand-bound structure of a tannase-like FAE. Our data reveal local conformational changes around the active site upon ligand binding, suggesting alternation between an active and a resting state of the enzyme. A swinging tyrosine residue appears to be gating the substrate binding pocket, while the lid domain of the protein exerts substrate specificity by means of a well-defined hydrophobic core that encases the phenyl moiety of the substrate.
Representative scheme of Tannase structure and an image from PDBsum server
no Image
Databases
PDB-Sum
8BHH Previously Class, Architecture, Topology and Homologous superfamily - PDB-Sum server
FSSP
8BHHFold classification based on Structure-Structure alignment of Proteins - FSSP server
