4XWL

Catalytic domain of Clostridium Cellulovorans Exgs

「4KIH」から置き換えられました

4XWL の概要

• エントリーDOI: 10.2210/pdb4xwl/pdb
• 関連するPDBエントリー: 4XWM 4XWN
• 分子名称: Exoglucanase S, DI(HYDROXYETHYL)ETHER, TETRAETHYLENE GLYCOL, ... (10 entities in total)
• 機能のキーワード: hydrolase
• 由来する生物種: Clostridium cellulovorans
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 78610.54

構造登録者

liaw, Y.-C. (登録日: 2015-01-29, 公開日: 2015-10-28, 最終更新日: 2023-11-08)

主引用文献

Tsai, L.-C.,Amiraslanov, I.,Chen, H.R.,Chen, Y.W.,Lee, H.L.,Liang, P.H.,Liaw, Y.-C.
Structures of exoglucanase from Clostridium cellulovorans: cellotetraose binding and cleavage
Acta Crystallogr.,Sect.F, 71:1264-1272, 2015

PubMed Abstract: Exoglucanase/cellobiohydrolase (EC 3.2.1.176) hydrolyzes a β-1,4-glycosidic bond from the reducing end of cellulose and releases cellobiose as the major product. Three complex crystal structures of the glycosyl hydrolase 48 (GH48) cellobiohydrolase S (ExgS) from Clostridium cellulovorans with cellobiose, cellotetraose and triethylene glycol molecules were solved. The product cellobiose occupies subsites +1 and +2 in the open active-site cleft of the enzyme-cellotetraose complex structure, indicating an enzymatic hydrolysis function. Moreover, three triethylene glycol molecules and one pentaethylene glycol molecule are located at active-site subsites -2 to -6 in the structure of the ExgS-triethylene glycol complex shown here. Modelling of glucose into subsite -1 in the active site of the ExgS-cellobiose structure revealed that Glu50 acts as a proton donor and Asp222 plays a nucleophilic role.

PubMed: 26457517
DOI: 10.1107/S2053230X15015915

実験手法

X-RAY DIFFRACTION (2.051 Å)