Open AccessOverproduction, purification, crystallization and preliminary X‐ray characterization of the C‐terminal family 65 carbohydrate‐binding module (CBM65B) of endoglucanase Cel5A from Eubacterium cellulosolvens
Author(s) -
Venditto Immacolata,
Baslé Arnaud,
Luís Ana S.,
Temple Max J.,
Ferreira Luís M. A.,
Fontes Carlos M. G. A.,
Gilbert Harry J.,
Najmudin Shabir
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113001620
Subject(s) - crystallization , eubacterium , cellulase , carbohydrate , chemistry , terminal (telecommunication) , crystallography , biochemistry , stereochemistry , enzyme , biology , organic chemistry , bacteria , genetics , computer science , telecommunications
The rumen anaerobic cellulolytic bacterium Eubacterium cellulosolvens produces a large range of cellulases and hemicellulases responsible for the efficient hydrolysis of plant cell wall polysaccharides. One of these enzymes, endoglucanase Cel5A, comprises a tandemly repeated carbohydrate‐binding module (CBM65) fused to a glycoside hydrolase family 5 (Cel5A) catalytic domain, joined by flexible linker sequences. The second carbohydrate‐binding module located at the C‐terminus side of the endoglucanase (CBM65B) has been co‐crystallized with either cellohexaose or xyloglucan heptasaccharide. The crystals belong to the hexagonal space group P 6 5 and tetragonal space group P 4 3 2 1 2, containing a single molecule in the asymmetric unit. The structures of CBM65B have been solved by molecular replacement.