3WMT
Crystal structure of feruloyl esterase B from Aspergillus oryzae
Summary for 3WMT
| Entry DOI | 10.2210/pdb3wmt/pdb |
| Descriptor | Probable feruloyl esterase B-1, 2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (4 entities in total) |
| Functional Keywords | alpha/beta-hydrolase fold, hydrolase, glycosylation, extracellular |
| Biological source | Aspergillus oryzae (Yellow koji mold) |
| Total number of polymer chains | 2 |
| Total formula weight | 115087.97 |
| Authors | Suzuki, K.,Ishida, T.,Igarashi, K.,Koseki, T.,Fushinobu, S. (deposition date: 2013-11-25, release date: 2014-08-06, Last modification date: 2024-10-09) |
| Primary citation | 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 Cited by 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: 25066066DOI: 10.1002/prot.24649 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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