Portal de Periódicos da CAPES

Overproduction, purification, crystallization and preliminary X-ray characterization of a novel carbohydrate-binding module of endoglucanase Cel5A from Eubacterium cellulosolvens

2011; Wiley; Volume: 67; Issue: 4 Linguagem: Inglês

10.1107/s1744309111004246

1744-3091

Ana S. Luís, Victor D. Alves, Maria João Romão, José A. M. Prates, C.M.G.A. Fontes, Shabir Najmudin,

Microbial Metabolites in Food Biotechnology

The anaerobic cellulolytic rumen bacterium Eubacterium cellulosolvens produces a large array of cellulases and hemicellulases that are responsible for the hydrolysis of plant cell-wall polysaccharides. One of these enzymes, endoglucanase Cel5A, comprises two tandemly repeated novel carbohydrate-binding modules (CBMs) and two catalytic domains belonging to glycoside hydrolase family 5 joined by flexible linker sequences. The novel CBM located at the N-terminus of the endoglucanase has been crystallized. The crystals belonged to the hexagonal space group P6122 and contained a single molecule in the asymmetric unit. The structure of the l-selenomethionine derivative has been solved by a MAD experiment on crystals that diffracted to 1.75 Å resolution.