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Figure 8 | BMC Biochemistry

Figure 8

From: Aglycone specificity of Thermotoga neapolitana β-glucosidase 1A modified by mutagenesis, leading to increased catalytic efficiency in quercetin-3-glucoside hydrolysis

Figure 8

Structural comparison of h CBG and Tn Bgl1A. Panel A and B show a surface view of h CBG (A.) and Tn Bgl1A (B.). The smaller entrance at the h CBG active site and wider entrance of the Tn Bgl1A active site are clearly visible. The overall similarity of the structures is shown by superimposition (C.) of the Tn Bgl1A (purple) and h CBG (blue) structures. The active site residues are shown as sticks. The fours loops surrounding the active site are indicated. Loops A (red), and B (orange) do not show differences but loop C (yellow in h CBG, cyan in Tn Bgl1A) and loop D (green in h CBG, cyan in Tn Bgl1A) presented big differences. Loop C, around the active site entrance, seems bigger in h CBG compared to Tn Bgl1A. Loop D on the other hand is long for Tn Bgl1A compared to the small and compact loop in h CBG. The β-strand close to the active site area (pink in Tn BglA, green in h CBG) was chosen for mutagenesis.

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BMC Biochemistry

ISSN: 1471-2091

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