4XWN

Complex structure of catalytic domain of Clostridium Cellulovorans Exgs and Cellotetraose

Replaces:  4KKK

Summary for 4XWN

• Entry DOI: 10.2210/pdb4xwn/pdb
• Related: 4XWL 4XWM
• Related PRD ID: PRD_900005 PRD_900016
• Descriptor: Exoglucanase S, beta-D-glucopyranose-(1-4)-beta-D-glucopyranose, beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: hydrolase
• Biological source: Clostridium cellulovorans
• Total number of polymer chains: 1
• Total formula weight: 77144.63

Authors

Liaw, Y.-C. (deposition date: 2015-01-29, release date: 2015-10-28, Last modification date: 2023-11-08)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.884 Å)