8IYB

Structure insight into substrate recognition and catalysis by feruloyl esterase from Aspergillus sydowii

Summary for 8IYB

• Entry DOI: 10.2210/pdb8iyb/pdb
• Related: 8IY8
• Descriptor: Feruloyl esterase, 2-acetamido-2-deoxy-beta-D-glucopyranose, 3-(4-HYDROXY-3-METHOXYPHENYL)-2-PROPENOIC ACID, ... (6 entities in total)
• Functional Keywords: feruloyl esterase, hydrolase
• Biological source: Aspergillus sydowii
• Total number of polymer chains: 2
• Total formula weight: 62575.00

Authors

Phienluphon, A.,Kondo, K.,Mikami, B.,Nagata, T.,Katahira, M. (deposition date: 2023-04-04, release date: 2023-10-25, Last modification date: 2024-11-13)

Primary citation

Phienluphon, A.,Kondo, K.,Mikami, B.,Nagata, T.,Katahira, M.
Structural insights into the molecular mechanisms of substrate recognition and hydrolysis by feruloyl esterase from Aspergillus sydowii.
Int.J.Biol.Macromol., 253:127188-127188, 2023

PubMed Abstract: The depolymerization of lignocellulosic biomass is facilitated by feruloyl esterases (FAEs), which hydrolyze ester bonds between lignin and polysaccharides. Fungal FAEs belonging to subfamily (SF) 6 release precursors such as ferulic acid derivatives, attractive for biochemical production. Among these, Aspergillus sydowii FAE (AsFaeE), an SF6 FAE, exhibits remarkable activity across various substrates. In this study, we conducted X-ray crystallography and kinetic analysis to unravel the molecular mechanisms governing substrate recognition and catalysis by AsFaeE. AsFaeE exhibits a typical α/β-hydrolase fold, characterized by a catalytic triad of serine, aspartate, and histidine. Comparative analysis of substrate-free, ferulic acid-bound, and sinapic acid-bound forms of AsFaeE suggests a conformational change in the loop covering the substrate-binding pocket upon binding. Notably, Pro158 and Phe159 within this loop cover the phenolic part of the substrate, forming three layers of planar rings. Our structure-based functional mutagenesis clarifies the roles of the residues involved in substrate binding and catalytic activity. Furthermore, distinct substrate-binding mechanisms between AsFaeE and other studied FAEs are identified. This investigation offers the initial structural insights into substrate recognition by SF6 FAEs, equipping us with structural knowledge that might facilitate the design of FAE variants capable of efficiently processing a wider range of substrate sizes.

PubMed: 37783244
DOI: 10.1016/j.ijbiomac.2023.127188

Experimental method

X-RAY DIFFRACTION (1.5 Å)