ePrints

Overproduction, purification, crystallization and preliminary X-ray characterization of the C-terminal family 65 carbohydrate-binding module (CBM65B) of endoglucanase Cel5A from Eubacterium cellulosolvens

Lookup NU author(s): Dr Max Temple, Emeritus Professor Harry Gilbert

Downloads

Full text for this publication is not currently held within this repository. Alternative links are provided below where available.

Abstract

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 P6(5) and tetragonal space group P4(3)2(1)2, containing a single molecule in the asymmetric unit. The structures of CBM65B have been solved by molecular replacement.

Publication metadata

Author(s): Venditto I, Basle A, Luis AS, Temple MJ, Ferreira LMA, Fontes CMGA, Gilbert HJ, Najmudin S

Publication type: Article

Publication status: Published

Journal: Acta Crystallographica. Section F: Structural Biology and Crystallization Communications

Year: 2013

Volume: 69

Pages: 191-194

Print publication date: 01/02/2013

ISSN (print): 1744-3091

ISSN (electronic):

Publisher: Wiley-Blackwell Publishing, Inc.

URL: http://dx.doi.org/10.1107/S1744309113001620

DOI: 10.1107/S1744309113001620

Altmetrics

Funding

Share