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Structures of Exoglucanase From Clostridium Cellulovorans: Cellotetraose Binding and Cleavage

Structures of Exoglucanase From Clostridium Cellulovorans: Cellotetraose Binding and Cleavage

Li Chu Tsai, Imamaddin Amiraslanov, Hung Ren Chen, Yun Wen Chen, Hsiao Lin Lee, Po Huang Liang, Yen Chywan Liaw

Acta Crystallogr F Struct Biol Commun. 2015 Oct;71(Pt 10):1264-72.

PMID: 26457517

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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP38819011	Cellotetraose		38819-01-1	Price

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