Publication

Article Metrics

Citations


Online attention

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

DOI: 10.1107/S1744309113001620 DOI Help
PMID: 23385766 PMID Help

Authors: Immacolata Venditto (Universidade Técnica de Lisboa) , Arnaud Basle (10.1107/S1744309113001620) , Ana S. Luís (Universidade Técnica de Lisboa) , Max J. Temple (Newcastle University) , Luís M. A. Ferreira (Universidade Técnica de Lisboa) , Carlos M. G. A. Fontes (Universidade Técnica de Lisboa) , Harry J. Gilbert (Newcastle University) , Shabir Najmudin
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology And Crystallization Communications , VOL 69 , PAGES 191 - 194

State: Published (Approved)
Published: February 2013

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 P65 and tetragonal space group P43212, containing a single molecule in the asymmetric unit. The structures of CBM65B have been solved by molecular replacement.

Journal Keywords: Eubacterium Cellulosolvens; Carbohydrate-Binding Module (Cbm65).

Subject Areas: Biology and Bio-materials


Instruments: I02-Macromolecular Crystallography

Added On: 05/02/2013 08:20

Discipline Tags:



Technical Tags: