Dimarogona_2020_FEBS.Lett_594_1738

Reference

Title : The crystal structure of a Fusarium oxysporum feruloyl esterase that belongs to the tannase family - Dimarogona_2020_FEBS.Lett_594_1738
Author(s) : Dimarogona M , Topakas E , Christakopoulos P , Chrysina ED
Ref : FEBS Letters , 594 :1738 , 2020
Abstract :

Feruloyl esterases are enzymes of industrial interest that catalyse the hydrolysis of the ester bond between hydroxycinnamic acids such as ferulic acid and sugars present in the plant cell wall. Although there are several structures of biochemically characterized feruloyl esterases available, the structural determinants of their substrate specificity are not yet fully understood. Here, we present the crystal structure of a feruloyl esterase from Fusarium oxysporum (FoFaeC) at 2.3 A resolution. Similar to the two other tannase-like feruloyl esterases, FoFaeC features a large lid domain covering the active site with potential regulatory role and a disulphide bond that brings together the serine and histidine of the catalytic triad. Differences are mainly observed in the metal coordination site and the substrate binding pocket. ENZYMES: E.C.3.1.1.73. DATABASES: The sequence of FoFaeC has been deposited with UniProt with accession code A0A1D3S5H0_FUSOX and the atomic coordinates of the three-dimensional structure with Protein Data Bank, with PDB code: 6FAT.

PubMedSearch : Dimarogona_2020_FEBS.Lett_594_1738
PubMedID: 32297315
Gene_locus related to this paper: fusox-a0a1d3s5h0

Related information

Gene_locus fusox-a0a1d3s5h0
Structure fusox-a0a1d3s5h0    6FAT

Citations formats

Dimarogona M, Topakas E, Christakopoulos P, Chrysina ED (2020)
The crystal structure of a Fusarium oxysporum feruloyl esterase that belongs to the tannase family
FEBS Letters 594 :1738

Dimarogona M, Topakas E, Christakopoulos P, Chrysina ED (2020)
FEBS Letters 594 :1738