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Figure 7
(a, b) Electrostatic (Coulomb) potential surface representations of (a) Bgl1 from C. saccharolyticus and (b) β-glucosidase from C. cellulovorans (PDB entry 3ahx); the colouring ranges from red for negative potential through white to blue for positive potential. (c, d) Hydrophobic surface representation of (c) Bgl1, also indicating the position of the bound (poly)ethylene glycol and glycerol molecules, and (d) β-glucosidase from C. cellulovorans (PDB entry 3ahx); the colouring ranges from dark cyan (most hydrophilic) to white to dark yellow (most lipophilic). (e) Superposition of the crystal structures of Bgl1 (red) and β-glucosidase from C. cellulovorans (PDB entry 3ahx; green); the regions in the two structures that exhibit the most profound differences are indicated with arrows (see Fig. 2[link] for the corresponding residues). The catalytic site of Bgl1 and an additional cavity adjacent to it that was detected by DeepSite (Jiménez et al., 2017BB18) are highlighted in surface representation (yellow).

Journal logoSTRUCTURAL
BIOLOGY
ISSN: 2059-7983
Volume 80| Part 10| October 2024| Pages 733-743
https://doi.org/10.1107/S2059798324009252
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