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Fig. 7 | Biotechnology for Biofuels

Fig. 7

From: Polysaccharide utilization loci-driven enzyme discovery reveals BD-FAE: a bifunctional feruloyl and acetyl xylan esterase active on complex natural xylans

Fig. 7

Comparison of substrate binding in BD-FAE (beige) and FAE from Anaeromyces mucronatus (AmCE1, PDB: 5CXX, green). The amino acid residues that were near the ligand were shown as sticks. The ligand was shown in pink and the hydrogen bonds of it were shown as dotted lines. A Fa-Araf docked into BD-FAE’s active site. B Complex structure of AmCE1a with ferulic acid. Surface representations of C BD-FAE and D AmCE1 showed that the active site of BD-FAE was more solvent exposed, whereas in AmCE1, the active site was more pocket like. Aliphatic residues on the surface of BD-FAE form a possible xylan-binding cleft, marked in blue

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