Abstract

The glycoside hydrolase family 3 (GH3) beta-glucosidases are a structurally diverse family of enzymes. Cel3A from Neurospora crassa (NcCel3A) belongs to a subfamily of key enzymes that are crucial for industrial biomass degradation. beta-Glucosidases hydrolyse the beta-1,4 bond at the nonreducing end of cellodextrins. The hydrolysis of cellobiose is of special importance as its accumulation inhibits other cellulases acting on crystalline cellulose. Here, the crystal structure of the biologically relevant dimeric form of NcCel3A is reported. The structure has been refined to 2.25 angstrom resolution, with an R-cryst and R-free of 0.18 and 0.22, respectively. NcCel3A is an extensively N-glycosylated glycoprotein that shares 46% sequence identity with Hypocrea jecorina Cel3A, the structure of which has recently been published, and 61% sequence identity with the thermophilic beta-glucosidase from Rasamsonia emersonii. NcCel3A is a three-domain protein with a number of extended loops that deepen the active-site cleft of the enzyme. These structures characterize this subfamily of GH3 beta-glucosidases and account for the high cellobiose specificity of this subfamily.

Keywords

glycoside hydrolase family 3; beta-glucosidase; biodegradation; crystal structure; Neurospora crassa; NcCel3A

Published in

Acta crystallographica. Section F, Structural biology communications
2018, volume: 74, pages: 787-796
Publisher: INT UNION CRYSTALLOGRAPHY

Authors' information