Crystallization and preliminary X‐ray diffraction analysis of a trimodular endo‐β‐1, 4‐glucanase (Cel5B) from Bacillus halodurans. Issue 12 (1st December 2014)

• Record Type: Journal Article
• Authors: Venditto, Immacolata; Santos, Helena; Sandy, James; Sanchez‐Weatherby, Juan; Ferreira, Luis M. A.; Sakka, Kazuo; Fontes, Carlos M. G. A.; Najmudin, Shabir
• Is Part Of: Acta crystallographica. Volume 70:Issue 12(2014:Dec.)
• Page Start: 1628
• Page End: 1630
• Publication Date: 2014-12-01
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X1402319X
• Languages: English
• ISSNs: 2053-230X

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>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, <italic>via</italic> linker sequences, to noncatalytic carbohydrate‐binding modules (CBMs). A putative modular endo‐β‐1, 4‐glucanase (<italic>Bh</italic>Cel5B) is encoded at locus BH0603 in the genome of <italic>Bacillus halodurans</italic>. 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 (<italic>Bh</italic>CBM46). Here, the crystallization and preliminary X‐ray diffraction analysis of the trimodular <italic>Bh</italic>Cel5B are reported. The crystals of <italic>Bh</italic>Cel5B belonged to the orthorhombic space group <italic>P</italic>2₁2₁ 2 and data were processed to a resolution of 1.64 Å. A molecular‐replacement solution has been found.</p> </abstract>