4WLC

Structure of dextran glucosidase with glucose

4WLC の概要

• エントリーDOI: 10.2210/pdb4wlc/pdb
• 分子名称: Glucan 1,6-alpha-glucosidase, beta-D-glucopyranose, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: glycoside hydrolase, dextran glucosidase, intermediate, complex, hydrolase
• 由来する生物種: Streptococcus mutans UA159
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 62549.42

構造登録者

Kobayashi, M.,Kato, K.,Yao, M. (登録日: 2014-10-07, 公開日: 2015-08-26, 最終更新日: 2024-10-23)

主引用文献

Kobayashi, M.,Saburi, W.,Nakatsuka, D.,Hondoh, H.,Kato, K.,Okuyama, M.,Mori, H.,Kimura, A.,Yao, M.
Structural insights into the catalytic reaction that is involved in the reorientation of Trp238 at the substrate-binding site in GH13 dextran glucosidase
Febs Lett., 589:484-489, 2015

PubMed Abstract: Streptococcus mutans dextran glucosidase (SmDG) belongs to glycoside hydrolase family 13, and catalyzes both the hydrolysis of substrates such as isomaltooligosaccharides and subsequent transglucosylation to form α-(1→6)-glucosidic linkage at the substrate non-reducing ends. Here, we report the 2.4Å resolution crystal structure of glucosyl-enzyme intermediate of SmDG. In the obtained structure, the Trp238 side-chain that constitutes the substrate-binding site turned away from the active pocket, concurrently with conformational changes of the nucleophile and the acid/base residues. Different conformations of Trp238 in each reaction stage indicated its flexibility. Considering the results of kinetic analyses, such flexibility may reflect a requirement for the reaction mechanism of SmDG.

PubMed: 25595454
DOI: 10.1016/j.febslet.2015.01.005

実験手法

X-RAY DIFFRACTION (2.402 Å)