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Purification, crystallization and crystallographic analysis of Clostridium thermocellum endo-1,4-β-D-xylanase 10B in complex with xylohexaose

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Resumo: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 P3221 and contain a dimer in the asymmetric unit. The crystals diffracted to beyond 2.0 Å resolution.
Autores principais:Najmudin, Shabir
Outros Autores:Pinheiro, Benedita A.; Romão, Maria J.; Prates, José A. M.; Fontes, Carlos M. G. A.
Assunto:Clostridium thermocellum Endo-1,4-β-D-xylanase 10B Structural Biology Biophysics Biochemistry Genetics Condensed Matter Physics
Ano:2008
País:Portugal
Tipo de documento:artigo
Tipo de acesso:acesso aberto
Instituição associada:Universidade Nova de Lisboa
Idioma:inglês
Origem:Repositório Institucional da UNL

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