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Structures of exoglucanase from Clostridium cellulovorans: cellotetraose binding and cleavage.


ABSTRACT: Exoglucanase/cellobiohydrolase (EC 3.2.1.176) hydrolyzes a ?-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.

SUBMITTER: Tsai LC 

PROVIDER: S-EPMC4601590 | biostudies-literature | 2015 Oct

REPOSITORIES: biostudies-literature

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Structures of exoglucanase from Clostridium cellulovorans: cellotetraose binding and cleavage.

Tsai Li Chu LC   Amiraslanov Imamaddin I   Chen Hung Ren HR   Chen Yun Wen YW   Lee Hsiao Lin HL   Liang Po Huang PH   Liaw Yen Chywan YC  

Acta crystallographica. Section F, Structural biology communications 20150923 Pt 10


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, indica  ...[more]

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