7DB5

Crystal structure of alpha-L-fucosidase from Vibrio sp. strain EJY3

7DB5 の概要

• エントリーDOI: 10.2210/pdb7db5/pdb
• 分子名称: Alpha-L-fucosidase, GLYCEROL, PHOSPHATE ION, ... (4 entities in total)
• 機能のキーワード: hydrolase
• 由来する生物種: Vibrio sp. EJY3
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 72184.24

構造登録者

Hong, H.,Kim, K.-J. (登録日: 2020-10-19, 公開日: 2021-03-24, 最終更新日: 2024-10-23)

主引用文献

Hong, H.,Kim, D.H.,Seo, H.,Kim, K.H.,Kim, K.J.
Dual alpha-1,4- and beta-1,4-Glycosidase Activities by the Novel Carbohydrate-Binding Module in alpha-l-Fucosidase from Vibrio sp. Strain EJY3.
J.Agric.Food Chem., 69:3380-3389, 2021

PubMed Abstract: Carbohydrates are structurally and functionally diverse materials including polysaccharides, and marine organisms are known to have many enzymes for the breakdown of complex polysaccharides. Here, we identified an α-l-fucosidase enzyme from the marine bacterium sp. strain EJY3 (FCD) that has dual α-1,4-glucosidic and β-1,4-galactosidic specificities. We determined the crystal structure of FCD and provided the structural basis underlying the dual α- and β-glycosidase activities of the enzyme. Unlike other three-domain FCDs, in FCD, carbohydrate-binding module-B (CBM-B) with a novel β-sandwich fold tightly contacts with the CatD/CBM-B main body and provides key residues for the β-1,4-glycosidase activity of the enzyme. The phylogenetic tree analysis suggests that only a few FCDs from marine microorganisms have the key structural features for dual α-1,4- and β-1,4-glycosidase activities. This study provides the structural insights into the mechanism underlying the novel glycoside hydrolase activities and could be applied for more efficient utilization in the hydrolysis of complex carbohydrates in biotechnological applications.

PubMed: 33705122
DOI: 10.1021/acs.jafc.0c08199

実験手法

X-RAY DIFFRACTION (1.9 Å)