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

Shabir Najmudin, Catarina I. P. D. Guerreiro, Luís M. A. Ferreira, Maria J. Romão, Carlos M. G. A. Fontes, José A. M. Prates

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Abstract

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.

Original languageEnglish
Pages (from-to)1043-1045
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume61
Issue number12
DOIs
Publication statusPublished - 1 Dec 2005

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