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Structural studies of a Glycoside Hydrolase Family 3 beta-glucosidase from the Model Fungus Neurospora crassaStructural studies of a Glycoside Hydrolase Family 3 beta-glucosidase from the Model Fungus Neurospora crassa
Structural highlights
FunctionPublication Abstract from PubMedThe 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 A resolution, with an Rcryst and Rfree 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. Structural studies of a glycoside hydrolase family 3 beta-glucosidase from the model fungus Neurospora crassa.,Karkehabadi S, Hansson H, Mikkelsen NE, Kim S, Kaper T, Sandgren M, Gudmundsson M Acta Crystallogr F Struct Biol Commun. 2018 Dec 1;74(Pt 12):787-796. doi:, 10.1107/S2053230X18015662. Epub 2018 Nov 26. PMID:30511673[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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