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![[Figure 6]](gm5108fig6mag.jpg)
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Figure 6
Left: superposition of the crystal structures of Bgl1 (shown in dark red) with its closest sequence and structural homologues β-glucosidase A from Clostridium cellulovorans (PDB entry 3ahx; cyan; Jeng et al., 2011  ), β-glucosidase from haemophilic Halothermothrix orenii strain H 168 (PDB entry 4ptv; pink; Hassan et al., 2015), β-glucosidase from Thermotoga maritima (PDB entry 1od0; light green; Zechel et al., 2003), β-glucosidase from T. neapolitana (PDB entry 5idi; orange; Kulkarni et al., 2017), β-glucosidase from Paenibacillus polymyxa (PDB entry 1tr1; grey; Sanz-Aparicio et al., 1998), β-glucosidase from Thermus thermophilus strain HB8 (PDB entry 4bce; magenta; Teze et al., 2014), β-glucosidase from Niallia circulans subsp. alkalophilus (PDB entry 1qox; khaki; Hakulinen et al., 2000), a metagenomic glucose-tolerant β-glucosidase (PDB entry 5xgz; blue; Matsuzawa et al., 2017) and β-glucosidase from Thermus nonproteolyticus (PDB entry 1np2; mauve; Wang et al., 2003). Right: close-up view of the active site indicating the catalytic site residues Glu163 and Glu361 (the numbering is from the Bgl1 structure). |
![[Figure 6]](gm5108fig6.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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