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International Union of Crystallography, Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 8(64), p. 715-718, 2008

DOI: 10.1107/s1744309108019696

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Purification, crystallization and crystallographic analysis ofClostridium thermocellumendo-1,4-β-D-xylanase 10B in complex with xylohexaose

Journal article published in 2008 by Shabir Najmudin, Benedita A. Pinheiro, Maria J. Romão, José A. M. Prates ORCID, Carlos M. G. A. Fontes
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This paper is available in a repository.

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Abstract

The cellulosome of Clostridium thermocellum is a highly organized multi-enzyme complex of cellulases and hemicellulases involved in the hydrolysis of plant cell-wall polysaccharides. The bifunctional multi-modular xylanase Xyn10B is one of the hemicellulase components of the C. thermocellum cellulosome. The enzyme contains an internal glycoside hydrolase family 10 catalytic domain (GH10) and a C-terminal family 1 carbohydrate esterase domain (CE1). The N-terminal moiety of Xyn10B (residues 32-551), comprising a carbohydrate-binding module (CBM22-1) and the GH10 E337A mutant, was crystallized in complex with xylohexaose. The crystals belong to the trigonal space group P3(2)21 and contain a dimer in the asymmetric unit. The crystals diffracted to beyond 2.0 A resolution.