title: Structure of the Catalytic Domain of α-L-Arabinofuranosidase from Coprinopsis cinerea, CcAbf62A, Provides Insights into Structure-Function Relationships in Glycoside Hydrolase Family 62.
abstract: α-L-Arabinofuranosidases, belonging to the glycoside hydrolase family (GH) 62, hydrolyze the α-1,2- or α-1,3-bond to liberate L-arabinofuranose from the xylan backbone. Here, we determined the structure of the C-terminal catalytic domain of CcAbf62A, a GH62 α-L-arabinofuranosidase from Coprinopsis cinerea. CcAbf62A is composed of a five-bladed β-propeller, as observed in other GH62 enzymes. The structure near the active site of CcAbf62A is also highly homologous to those of other GH62 enzymes. However, a calcium atom in the catalytic center interacts with an asparagine residue, Asn279, which is not found in other GH62 enzymes. In addition, some residues in subsites +3R, +2NR, +3NR, and +4NR of CcAbf62A are not conserved in other GH62 enzymes. In particular, a histidine residue, His221, is uniquely observed in subsite +2NR of CcAbf62A, which is likely to influence the substrate specificity. The results obtained here suggest that the amino acid residues that interact with the xylan backbone vary among the GH62 enzymes, despite the high similarity of their overall structures.
authors: Department of Applied Biological Science, Tokyo University of Agriculture and Technology, Tokyo, 183-8509, Japan. tonozuka@cc.tuat.ac.jp.
authors: Takashi
authors: http://orcid.org/0000-0002-5422-7548
authors: T
authors: Tonozuka
authors: Department of Applied Biological Science, Tokyo University of Agriculture and Technology, Tokyo, 183-8509, Japan.
authors: Yutaro
authors: Y
authors: Tanaka
authors: Department of Applied Biological Science, Tokyo University of Agriculture and Technology, Tokyo, 183-8509, Japan.
authors: Shunsaku
authors: S
authors: Okuyama
authors: Department of Applied Biological Science, Tokyo University of Agriculture and Technology, Tokyo, 183-8509, Japan.|Research Institute of Green Science and Technology, Shizuoka University, Shizuoka, 422-8529, Japan.
authors: Takatsugu
authors: T
authors: Miyazaki
authors: Department of Applied Biological Science, Tokyo University of Agriculture and Technology, Tokyo, 183-8509, Japan.
authors: Atsushi
authors: A
authors: Nishikawa
authors: Department of Environmental and Natural Resource Science, Tokyo University of Agriculture and Technology, Tokyo, 183-8509, Japan.
authors: Makoto
authors: M
authors: Yoshida
mesh_terms: D000595:Amino Acid Sequence; D001487:Basidiomycota / Q000201:enzymology*; D002384:Catalysis; D004789:Enzyme Activation; D006026:Glycoside Hydrolases; D008956:Models, Chemical; D008958:Models, Molecular; D062105:Molecular Docking Simulation; D008969:Molecular Sequence Data; D011487:Protein Conformation; D000072417:Protein Domains; D013329:Structure-Activity Relationship
chemical_list: D006026:Glycoside Hydrolases; C019713:alpha-N-arabinofuranosidase
keywords: Arabinoxylan; Coprinopsis cinerea; GH62; Hemicellulose; α-L-arabinofuranosidase