3WMT

Crystal structure of feruloyl esterase B from Aspergillus oryzae

3WMT の概要

• エントリーDOI: 10.2210/pdb3wmt/pdb
• 分子名称: Probable feruloyl esterase B-1, 2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: alpha/beta-hydrolase fold, hydrolase, glycosylation, extracellular
• 由来する生物種: Aspergillus oryzae (Yellow koji mold)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 115087.97

構造登録者

Suzuki, K.,Ishida, T.,Igarashi, K.,Koseki, T.,Fushinobu, S. (登録日: 2013-11-25, 公開日: 2014-08-06, 最終更新日: 2024-10-09)

主引用文献

Suzuki, K.,Hori, A.,Kawamoto, K.,Thangudu, R.R.,Ishida, T.,Igarashi, K.,Samejima, M.,Yamada, C.,Arakawa, T.,Wakagi, T.,Koseki, T.,Fushinobu, S.
Crystal structure of a feruloyl esterase belonging to the tannase family: a disulfide bond near a catalytic triad.
Proteins, 82:2857-2867, 2014

PubMed Abstract: Feruloyl esterase (FAE) catalyzes the hydrolysis of the ferulic and diferulic acids present in plant cell wall polysaccharides, and tannase catalyzes the hydrolysis of tannins to release gallic acid. The fungal tannase family in the ESTHER database contains various enzymes, including FAEs and tannases. Despite the importance of FAEs and tannases in bioindustrial applications, three-dimensional structures of the fungal tannase family members have been unknown. Here, we determined the crystal structure of FAE B from Aspergillus oryzae (AoFaeB), which belongs to the fungal tannase family, at 1.5 Å resolution. AoFaeB consists of a catalytic α/β-hydrolase fold domain and a large lid domain, and the latter has a novel fold. To estimate probable binding models of substrates in AoFaeB, an automated docking analysis was performed. In the active site pocket of AoFaeB, residues responsible for the substrate specificity of the FAE activity were identified. The catalytic triad of AoFaeB comprises Ser203, Asp417, and His457, and the serine and histidine residues are directly connected by a disulfide bond of the neighboring cysteine residues, Cys202 and Cys458. This structural feature, the "CS-D-HC motif," is unprecedented in serine hydrolases. A mutational analysis indicated that the novel structural motif plays essential roles in the function of the active site.

PubMed: 25066066
DOI: 10.1002/prot.24649

実験手法

X-RAY DIFFRACTION (1.5 Å)