Fig. 1: Structure, phylogeny and substrate specificity of endo−1,3-fucanases from the GH168 family. | Nature Communications

Fig. 1: Structure, phylogeny and substrate specificity of endo−1,3-fucanases from the GH168 family.

From: Structure-function relationship of the GH168 fucanase reveals an unusual enzyme recognition mechanism for sulfated polysaccharide

Fig. 1: Structure, phylogeny and substrate specificity of endo−1,3-fucanases from the GH168 family.

a Overall fold of WfGH168_II. The numbers of the secondary structure elements are indicated. b Hydrophobic interface between the β-sheet subdomain and the catalytic domain, featuring khaki sticks to denote the residues mediating domain association. c Superposition of representative structures from the four fucan-active enzyme family. The similar residues at the −1 subsite are shown as sticks. All residues are conserved, except for the W136 residue within the GH168 family, which may occasionally be substituted by tyrosine, which also possesses an aromatic ring. d Phylogenetic analysis of the GH168 family. e Clustering results of degradation degree of sulfated fucans by the GH168 enzymes.

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