The structure investigation of GH174 endo-1,3-fucanase revealed an unusual glycoside hydrolase fold.

ABSTRACT

Sulfated fucan has attracted increasing research interest due to its various biological activities. Endo-1,3-fucanases are favorable tools for structure investigation and structure-activity relationships establishment of sulfated fucan. However, the three-dimensional structure of enzymes from the GH174 family has not been disclosed, which hinders the understanding of the action mechanism. This study reports the first crystal structure of endo-1,3-fucanase from GH174 family (Fun174A) at a resolution of 1.60 Å. Notably, Fun174A exhibited an unusual distorted ß-sandwich fold, which is distinct from other known glycoside hydrolase folds. The conserved amino acid residues D119 and H154 were proposed as the catalytic residues in the family. Molecular docking suggested that Fun174A primarily recognized sulfated fucan through a series of polar amino acid residues around the substrate binding pocket. Furthermore, structural bioinformatics analysis suggested that the structural analogs of Fun174A may be extensively implicated in the bacterial metabolism of polysaccharides, which provided opportunities for the discovery of novel glycoside hydrolases. This study offers new insights into the structural diversity of glycoside hydrolases and will contribute to the establishment of a novel clan of glycoside hydrolases.