title: Crystal structure of the N-terminal domain of a glycoside hydrolase family 131 protein from Coprinopsis cinerea.
abstract: The crystal structure of the N-terminal putative catalytic domain of a glycoside hydrolase family 131 protein from Coprinopsis cinerea (CcGH131A) was determined. The structure of CcGH131A was found to be composed of a β-jelly roll fold and mainly consisted of two β-sheets, sheet-A and sheet-B. A concave of sheet-B, the possible active site, was wide and shallow, and three glycerol molecules were present in the concave. Arg96, Glu98, Glu138, and His218 are likely to be catalytically critical residues, and it was suggested that the catalytic mechanism of CcGH131A is different from that of typical glycosidases.
authors.affiliation: Department of Applied Biological Science, Tokyo University of Agriculture and Technology, Tokyo 183-8509, Japan.
authors.forename: Takatsugu
authors.initials: T
authors.lastname: Miyazaki
authors.forename: Makoto
authors.initials: M
authors.lastname: Yoshida
authors.forename: Mizuki
authors.initials: M
authors.lastname: Tamura
authors.forename: Yutaro
authors.initials: Y
authors.lastname: Tanaka
authors.forename: Kiwamu
authors.initials: K
authors.lastname: Umezawa
authors.forename: Atsushi
authors.initials: A
authors.lastname: Nishikawa
authors.forename: Takashi
authors.initials: T
authors.lastname: Tonozuka
mesh_terms: D000363:Agaricales / Q000201:enzymology*; D000595:Amino Acid Sequence; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D005656:Fungal Proteins / Q000737:chemistry*; D006026:Glycoside Hydrolases / Q000737:chemistry*; D006860:Hydrogen Bonding; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary
chemical_list: D005656:Fungal Proteins; D006026:Glycoside Hydrolases