Overexpression, purification and crystallization of the two C-terminal domains of the bifunctional cellulase ctCel9D-Cel44A from Clostridium thermocellum

Clostridium thermocellum produces a highly organized multi-enzyme complex of cellulases and hemicellulases for the hydrolysis of plant cell-wall polysaccharides, which is termed the cellulosome. The bifunctional multi-modular cellulase ctCel9D-Cel44A is one of the largest components of the C. thermo...

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Bibliographic Details
Main Author: Najmudin, Shabir (author)
Other Authors: Guerreiro, Catarina I. P. D. (author), Ferreira, Luís M. A. (author), Romão, Maria J. (author), Fontes, Carlos M. G. A. (author), Prates, José A. M. (author)
Format: article
Language:eng
Published: 2019
Subjects:
Online Access:https://doi.org/10.1107/S1744309105035670
Country:Portugal
Oai:oai:run.unl.pt:10362/63001
Description
Summary:Clostridium thermocellum produces a highly organized multi-enzyme complex of cellulases and hemicellulases for the hydrolysis of plant cell-wall polysaccharides, which is termed the cellulosome. The bifunctional multi-modular cellulase ctCel9D-Cel44A is one of the largest components of the C. thermocellum cellulosome. The enzyme contains two internal catalytic domains belonging to glycoside hydrolase families 9 and 44. The C-terminus of this cellulase, comprising a polycystic kidney-disease module (PKD) and a carbohydrate-binding module (CBM44), has been crystallized. The crystals belong to the tetragonal space group P43232, containing a single molecule in the asymmetric unit. Native and seleno-l-methionine-derivative crystals diffracted to 2.1 and 2.8 Å, respectively.