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Fig. 8 | Biotechnology for Biofuels

Fig. 8

From: Chaetomella raphigera β-glucosidase D2-BGL has intriguing structural features and a high substrate affinity that renders it an efficient cellulase supplement for lignocellulosic biomass hydrolysis

Fig. 8

Crystal structure analysis indicates that D2-BGL is a GH3 β-glucosidase with specific glycosylation sites. a β-Glucosidase D2-BGL consists of a TIM barrel-like domain (in red), an α/β sandwich domain (in green), and a fibronectin type III-like domain (in yellow). D232 and E442, which are represented by pink spheres, indicate the location of the catalytic center. b Structure superposition reveals that three extra insertion domains (in black) observed in the Aspergillus aculeatus β-glucosidase AaBGL1 (in grey) are absent from D2-BGL (in orange). c Glycosylation sites are determined by the presence of N-acetyl glucosamine at residues N68, N205 and N273 for N-glycosylation and by a mannose at T431 for O-glycosylation. N68 and T431 glycosylation have not been observed in any other reported GH3 β-glucosidases

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