Figure 3 | Scientific Reports

Figure 3

From: Crystal structure and substrate interactions of an unusual fungal non-CBM carrying GH26 endo-β-mannanase from Yunnania penicillata

Figure 3

Sequence alignment of the catalytic GH26 core region from 9 fungal GH26 endomannanases. Secondary structure elements for YpenMan26A and PansMan26A are displayed above and below the alignment respectively. Mutated residues D37 and W110 (lilac) and residues involved in ligand binding (red stars) in the YpenMan26A structure including the two catalytic residues. The α-helix in PansMan26A (α9) which is nearest the CBM35 and which is a surface loop in YpenMan26A is coloured blue. Identical residues are shown in white on red background. Highly similar residues (when the similarity score assigned to one column is above 0.7) are coloured red and framed in a blue box. The GH26 core sequence of YpenMan26A (AYU65281), AnidMan26A (Q5AWB7), Ascobolus stictoideus AstiMan26A (BBW45412), Collariella virescens CvirMan26A (BBW45415), Mycothermus thermophiles MtheMan26A (MH208368), Neoascochyta desmazieri NdesMan26A (MH208367), Myceliophthora thermophila MtMan26A (99077), Wsp.Man26A (MH208369), PansMan26A (B2AEP0) were aligned by MUSCLE55 and the figure was generated using ESPript 3 Web server56.

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