3wmt | pdb_00003wmt

Crystal structure of feruloyl esterase B from Aspergillus oryzae

spinqualitylabelsall models 3wmt, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3wmt is a 2 chain structure with sequence from Aspergillus oryzae RIB40. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.5Å Ligands: CA, NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function FAEB1_ASPOR Involved in degradation of plant cell walls. Hydrolyzes of the feruloyl-arabinose ester bond in arabinoxylans as well as the feruloyl-galactose and feruloyl-arabinose ester bonds in pectin (By similarity). Publication Abstract from PubMed 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 A resolution. AoFaeB consists of a catalytic alpha/beta-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. Crystal structure of a feruloyl esterase belonging to the tannase family: a disulfide bond near a catalytic triad.,Suzuki K, Hori A, Kawamoto K, Thangudu RR, Ishida T, Igarashi K, Samejima M, Yamada C, Arakawa T, Wakagi T, Koseki T, Fushinobu S Proteins. 2014 Oct;82(10):2857-67. doi: 10.1002/prot.24649. Epub 2014 Aug 11. PMID:25066066 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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