Crystallization and preliminary X-ray diffraction analysis of a trimodular endo-[beta]-1,4-glucanase (Cel5B) from Bacillus halodurans

DOI: 10.1107/S2053230X1402319X
PMID: 25484213

Authors: Immacolata Venditto (CIISA, Faculdade de Medicina Veterinaria, Universidade de Lisboa) , Helena Santos (CIISA, Faculdade de Medicina Veterinaria, Universidade de Lisboa) , James Sandy (Diamond Light Source) , Juan Sanchez-Weatherby (Diamond Light Source) , Luis M. A. Ferreira (CIISA, Faculdade de Medicina Veterinaria, Universidade de Lisboa) , Kazuo Sakka (Graduate School of Bioresources, Mie University) , Carlos M. G. A. Fontes (CIISA, Faculdade de Medicina Veterinaria, Universidade de Lisboa) , Shabir Najmudin (CIISA, Faculdade de Medicina Veterinaria, Universidade de Lisboa)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology Communications , VOL 70 , PAGES 1628 - 1630

State: Published (Approved)
Published: December 2014

Abstract: Cellulases catalyze the hydrolysis of cellulose, the major constituent of plant biomass and the most abundant organic polymer on earth. Cellulases are modular enzymes containing catalytic domains connected, via linker sequences, to noncatalytic carbohydrate-binding modules (CBMs). A putative modular endo-[beta]-1,4-glucanase (BhCel5B) is encoded at locus BH0603 in the genome of Bacillus halodurans. It is composed of an N-terminal glycoside hydrolase family 5 catalytic module (GH5) followed by an immunoglobulin-like module and a C-terminal family 46 CBM (BhCBM46). Here, the crystallization and preliminary X-ray diffraction analysis of the trimodular BhCel5B are reported. The crystals of BhCel5B belonged to the orthorhombic space group P2121 2 and data were processed to a resolution of 1.64 Å. A molecular-replacement solution has been found.

Journal Keywords: endo-β-1,4-glucanase Cel5B; family 5 glycoside hydrolase (GH5); family 46 carbohydrate-binding module (CBM46); plant cell-wall degradation; Bacillus halodurans

Diamond Keywords: Enzymes

Subject Areas: Biology and Bio-materials


Instruments: I02-Macromolecular Crystallography , I04-Macromolecular Crystallography

Added On: 06/02/2015 09:01

Discipline Tags:

Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)