5NBS

Structural studies of a Glycoside Hydrolase Family 3 beta-glucosidase from the Model Fungus Neurospora crassa

Summary for 5NBS

• Entry DOI: 10.2210/pdb5nbs/pdb
• Descriptor: Beta-glucosidase, alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (10 entities in total)
• Functional Keywords: glycoside hydrolase, beta-glucosidase, biodegradation, neurospora crassa, hydrolase
• Biological source: Neurospora crassa OR74A
• Total number of polymer chains: 2
• Total formula weight: 203149.17

Authors

Gudmundsson, M.,Karkehabadi, S.,Kaper, T.,Sandgren, M. (deposition date: 2017-03-02, release date: 2018-03-21, Last modification date: 2024-11-20)

Primary citation

Karkehabadi, S.,Hansson, H.,Mikkelsen, N.E.,Kim, S.,Kaper, T.,Sandgren, M.,Gudmundsson, M.
Structural studies of a glycoside hydrolase family 3 beta-glucosidase from the model fungus Neurospora crassa.
Acta Crystallogr F Struct Biol Commun, 74:787-796, 2018

PubMed Abstract: The glycoside hydrolase family 3 (GH3) β-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. β-Glucosidases hydrolyse the β-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 Å resolution, with an R and R 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 β-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 β-glucosidases and account for the high cellobiose specificity of this subfamily.

PubMed: 30511673
DOI: 10.1107/S2053230X18015662

Experimental method

X-RAY DIFFRACTION (2.25 Å)