5Z9S

Functional and Structural Characterization of a beta-Glucosidase Involved in Saponin Metabolism from Intestinal Bacteria

5Z9S の概要

• エントリーDOI: 10.2210/pdb5z9s/pdb
• 分子名称: Glycosyl hydrolase family 3 protein, beta-D-glucopyranose (3 entities in total)
• 機能のキーワード: saponins, glucosidase, biotransformation, bifidobacterium longum, hydrolase
• 由来する生物種: Bifidobacterium longum
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 172323.64

構造登録者

Yan, S.,Wei, P.C.,Li, J.R. (登録日: 2018-02-05, 公開日: 2018-03-14, 最終更新日: 2023-11-22)

主引用文献

Yan, S.,Wei, P.C.,Chen, Q.,Chen, X.,Wang, S.C.,Li, J.R.,Gao, C.
Functional and structural characterization of a beta-glucosidase involved in saponin metabolism from intestinal bacteria.
Biochem. Biophys. Res. Commun., 496:1349-1356, 2018

PubMed Abstract: Saponins are natural glycosides widely used in medicine and the food industry. Although saponin metabolism in human is dependent on intestinal microbes, few involving bacteria enzymes have been identified. We cloned BlBG3, a GH3 β-glucosidase from Bifidobacterium longum, from human stool. We found that BlBG3 catalyzes the hydrolysis of glycoside furostanol and ginsenoside Rb1 at higher efficiency than other microbial β-glucosidases. Structural analysis of BlBG3 in complex with d-glucose revealed its three unique loops, which form a deep pocket and participate in substrate binding. To understand how substrate is bound to the pocket, molecular docking was performed and the binding interactions of protobioside with BlBG3 were revealed. Mutational study suggested that R484 and H642 are critical for enzymatic activity. Our study presents the first structural and functional analysis of a saponin-processing enzyme from human microbiota.

PubMed: 29421652
DOI: 10.1016/j.bbrc.2018.02.018

実験手法

X-RAY DIFFRACTION (2.3 Å)