Open AccessOverexpression, purification and crystallization of the two C‐terminal domains of the bifunctional cellulase ct Cel9D‐Cel44A from Clostridium thermocellum
Author(s) -
Najmudin Shabir,
Guerreiro Catarina I. P. D.,
Ferreira Luís M. A.,
Romão Maria J. C.,
Fontes Carlos M. G. A.,
Prates José A. M.
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105035670
Subject(s) - clostridium thermocellum , cellulase , cellulosome , glycoside hydrolase , chemistry , biochemistry , hydrolysis , hydrolase , cellulose , enzyme , crystallography
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 ct Cel9D‐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 P 4 3 2 1 2, containing a single molecule in the asymmetric unit. Native and seleno‐ l ‐methionine‐derivative crystals diffracted to 2.1 and 2.8 Å, respectively.