Unknown

Dataset Information

0

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

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.

SUBMITTER: Najmudin S 

PROVIDER: S-EPMC2494957 | biostudies-literature | 2008 Aug

REPOSITORIES: biostudies-literature

Json Xml
altmetric image

Publications

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

Najmudin Shabir S   Pinheiro Benedita A BA   Romão Maria J MJ   Prates José A M JA   Fontes Carlos M G A CM  

Acta crystallographica. Section F, Structural biology and crystallization communications 20080705 Pt 8

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 32-55  ...[more]

Similar Datasets

Unknown Purification, Identification, and Characterization of an Endo-1,4-?-Xylanase from Wheat Malt.
| S-EPMC7180899 | biostudies-literature
Unknown Identification of an endo-1,4-beta-xylanase of Ustilago maydis.
| S-EPMC3737115 | biostudies-literature
Unknown Computational design of an endo-1,4-beta-xylanase ligand binding site.
| S-EPMC3092692 | biostudies-literature
Unknown Identification of an endo-beta-1,4-D-xylanase from Magnaporthe grisea by gene knockout analysis, purification, and heterologous expression.
| S-EPMC1392926 | biostudies-literature
Unknown Non-Specific GH30_7 Endo-β-1,4-xylanase from <i>Talaromyces leycettanus</i>.
| S-EPMC8347862 | biostudies-literature
Unknown Crystallization and preliminary X-ray analysis of a cold-active endo-β-1,4-D-xylanase from glycoside hydrolase family 8.
| S-EPMC3079997 | biostudies-literature
Unknown Purification and characterization of an endoglucanase (1,4-beta-D-glucan glucanohydrolase) from Clostridium thermocellum.
| S-EPMC1163377 | biostudies-other
Unknown Overexpression, crystallization and preliminary X-ray crystallographic analysis of glucuronoxylan xylanohydrolase (Xyn30A) from Clostridium thermocellum.
| S-EPMC3855739 | biostudies-literature
Unknown Purification, crystallization and preliminary X-ray characterization of the pentamodular arabinoxylanase CtXyl5A from Clostridium thermocellum.
| S-EPMC3144809 | biostudies-literature
Unknown Xylanase B from Clostridium cellulovorans 743B: overexpression, purification, crystallization and X-ray diffraction analysis.
| S-EPMC5947682 | biostudies-literature