4HZ8

Crystal structure of BglB with natural substrate

「3FJ0」から置き換えられました

4HZ8 の概要

• エントリーDOI: 10.2210/pdb4hz8/pdb
• 関連するPDBエントリー: 4HZ6 4HZ7
• 分子名称: Beta-glucosidase, beta-D-glucopyranose (3 entities in total)
• 機能のキーワード: glucosidase, beta-glucosidase, bglb, bgl, hydrolase, glycosidase, tim barrel, carbohydrate/sugar binding
• 由来する生物種: Uncultured bacterium
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 50474.43

構造登録者

Hwang, K.Y.,Nam, K.H. (登録日: 2012-11-14, 公開日: 2012-12-19, 最終更新日: 2023-11-08)

主引用文献

Nam, K.H.,Sung, M.W.,Hwang, K.Y.
Structural insights into the substrate recognition properties of beta-glucosidase.
Biochem.Biophys.Res.Commun., 391:1131-1135, 2010

PubMed Abstract: Beta-glucosidase enzymes (EC 3.2.1-3.2.3) hydrolyze sugars and are implicated in a wide spectrum of biological processes. Recently, we reported that beta-glucosidase has varied kinetic parameters for the natural and synthetic substrates [K.H Nam, S.J. Kim, M.Y. Kim, J.H. Kim, T.S. Yeo, C.M. Lee, H.K Jun, K.Y. Hwang. Crystal structure of engineered beta-glucosidase from a soil metagenome, Proteins 73 (2008) 788-793]. However, an understanding of the kinetic values of beta-glucosidase has not yet enabled the elucidation of its molecular function. Here, we report the X-ray crystal structure of beta-glucosidase with a glucose and cellobiose fragment from uncultured soil metagenome. From the various crystals, we obtained the pre-reaction (native), intermediate (disaccharide cleavage) and post-reaction (glucose binding) states of the active site pocket. These structures provide snapshots of the catalytic processing of beta-glucosidase. In addition, the intermediate state of the crystal structure provides insight into the substrate specificity of beta-glucosidase. These structural studies will facilitate elucidation of the architectural mechanism responsible for the substrate recognition of beta-glucosidase.

PubMed: 20005197
DOI: 10.1016/j.bbrc.2009.12.038

実験手法

X-RAY DIFFRACTION (1.14 Å)