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