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Fig. 1 | Biotechnology for Biofuels

Fig. 1

From: Insight into the functional roles of Glu175 in the hyperthermostable xylanase XYL10C-ΔN through structural analysis and site-saturation mutagenesis

Fig. 1

The overall structure and active-site architecture of the XYL10C-ΔN-xylobiose complex. a The crystal structure of XYL10C-xylobiose complex. The typical (β/α)8 barrel fold of XYL10C-ΔN with α-helices (cyan), β-strands (violet) and loops (pink) indicated. The loops at the C-terminus of the β-strands form a salad bowl-shaped groove that accounts for the endo-mode action against polymeric substrates. The catalytic residues Glu219 and Glu332, located on strands β4 and β7, are involved in substrate recognition and catalysis. b The electron density map. c Xylobiose (green) binding in the active site of XYL10C-ΔN. Catalytic residues are indicated in red. Amino acids that are important for to bind xylobiose residues in the subsites are indicated. d Structural comparison of XYL10C-ΔN and XylE (PDB: 4F8X; green). The amino acids of XylE are shown in brackets

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