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Structural snapshot of a glycoside hydrolase family 8 endo-beta-1,4-giucanase capturing the state after cleavage of the scissile bond

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Title: Structural snapshot of a glycoside hydrolase family 8 endo-beta-1,4-giucanase capturing the state after cleavage of the scissile bond
Authors: Fujiwara, Takaaki Browse this author
Fujishima, Ayumi Browse this author
Nakamura, Yui Browse this author
Tajima, Kenji Browse this author
Yao, Min Browse this author →KAKEN DB
Keywords: bacterial cellulose
crystal structure
Issue Date: 2022
Publisher: International Union of Crystallography
Journal Title: Acta Crystallographica Section D-structural Biology
Volume: 78
Start Page: 228
End Page: 237
Publisher DOI: 10.1107/S2059798321012882
Abstract: Bacterial cellulose (BC), which is produced by bacteria, is a biodegradable and biocompatible natural resource. Because of its remarkable physicochemical properties, BC has attracted attention for the development and manufacture of biomedical and industrial materials. In the BC production system, the enzyme endo-beta-1,4-glucanase, which belongs to glycoside hydrolase family 8 (GH8), acts as a cleaner by trimming disordered cellulose fibers to produce high-quality BC. Understanding the molecular mechanism of the endo-beta-1,4-glucanase would help in developing a reasonable biosynthesis of BC. Nevertheless, all of the steps in the reaction of this endo-beta-1,4-glucanase are not clear. This study confirms the BC hydrolytic activity of the endo-beta-1,4-glucanase from the BC-producing bacterium Enterobacter sp. CJF-002 (EbBcsZ) and reports crystal structures of EbBcsZ. Unlike in previously reported GH8 endo-beta-1,4-glucanase structures, here the base catalyst was mutated (D242A) and the structure of this mutant bound to cellooligosaccharide [EbBcsZ(D242A)(CPT)] was analyzed. The EbBcsZ (D242A)(CPT) structure showed two cellooligosaccharides individually bound to the plus and minus subsites of EbBcsZ. The glucosyl unit in subsite -1 presented a distorted S-5(1) conformation, a novel snapshot of a state immediately after scissile-bond cleavage. In combination with previous studies, the reaction process of endo-beta-1,4-glucanase is described and the beta-1,4-glucan-trimming mechanism of EbBcsZ is proposed. The EbBcsZ(D242A)(CPT) structure also showed an additional beta-1,4-glucan binding site on the EbBcsZ surface, which may help to accept the substrate.
Type: article
Appears in Collections:生命科学院・先端生命科学研究院 (Graduate School of Life Science / Faculty of Advanced Life Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

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