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Fig. 9 | Microbial Cell Factories

Fig. 9

From: Isolation, expression, and in silico profiling of a thermostable xylanase from Geobacillus stearothermophilus strain NASA267: insights into structural features and agro-waste valorization

Fig. 9

Overall structure and active site representation of xyl267. The typical (β/α)₈ barrel fold is shown, with α-helices in cyan and β-strands in magenta. The catalytic triad residues, Glu134 and Glu241, are highlighted in green (A). A side view of the ribbon diagram illustrating the “salad-bowl” shape, a characteristic feature of GH10 family members (B). The surface topology of the enzyme, revealing an extended groove suitable for accommodating polymeric substrates, consistent with its endo-mode of action (C)

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Microbial Cell Factories

ISSN: 1475-2859

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