Ferousi_2023_FEBS.Lett_597_1415

Reference

Title : Crystal structure of the Fusarium oxysporum tannase-like feruloyl esterase FaeC in complex with p-coumaric acid provides insight into ligand binding - Ferousi_2023_FEBS.Lett_597_1415
Author(s) : Ferousi C , Kosinas C , Nikolaivits E , Topakas E , Dimarogona M
Ref : FEBS Letters , 597 :1415 , 2023
Abstract :

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.

PubMedSearch : Ferousi_2023_FEBS.Lett_597_1415
PubMedID: 36961270
Gene_locus related to this paper: fusox-a0a1d3s5h0

Related information

Substrate p-coumaric-acid
Gene_locus p-coumaric-acid    fusox-a0a1d3s5h0
Structure p-coumaric-acid    fusox-a0a1d3s5h0    8BHH

Citations formats

Ferousi C, Kosinas C, Nikolaivits E, Topakas E, Dimarogona M (2023)
Crystal structure of the Fusarium oxysporum tannase-like feruloyl esterase FaeC in complex with p-coumaric acid provides insight into ligand binding
FEBS Letters 597 :1415

Ferousi C, Kosinas C, Nikolaivits E, Topakas E, Dimarogona M (2023)
FEBS Letters 597 :1415