Crystal structure of the N-terminal domain of a glycoside hydrolase family 131 protein from Coprinopsis cinerea

• The structure of the N-terminal domain of a GH131 protein was determined.
• The structure is composed of a β-jelly roll fold.
• The possible active site is wide and shallow.
• Arg96, Glu98, Glu138, and His218 are likely to be catalytically critical.
• The catalytic mechanism could be different from that of typical glycosidases.

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.