Overexpression, purification and crystallization of the two C-terminal domains of the bifunctional cellulase ctCel9D-Cel44A from Clostridium thermocellum

Najmudin, Shabir; Guerreiro, Catarina I. P. D.; Ferreira, Luís M. A.; Romão, Maria J.; Fontes, Carlos M. G. A.; Prates, José A. M.

http://hdl.handle.net/10362/63001

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Autores

Najmudin, Shabir

Guerreiro, Catarina I. P. D.

Ferreira, Luís M. A.

Romão, Maria J.

Fontes, Carlos M. G. A.

Prates, José A. M.

Resumo(s)

Clostridium thermocellum produces a highly organized multi-enzyme complex of cellulases and hemicellulases for the hydrolysis of plant cell-wall polysaccharides, which is termed the cellulosome. The bifunctional multi-modular cellulase ctCel9D-Cel44A is one of the largest components of the C. thermocellum cellulosome. The enzyme contains two internal catalytic domains belonging to glycoside hydrolase families 9 and 44. The C-terminus of this cellulase, comprising a polycystic kidney-disease module (PKD) and a carbohydrate-binding module (CBM44), has been crystallized. The crystals belong to the tetragonal space group P43232, containing a single molecule in the asymmetric unit. Native and seleno-l-methionine-derivative crystals diffracted to 2.1 and 2.8 Å, respectively.

Palavras-chave

Biophysics Structural Biology Biochemistry Genetics Condensed Matter Physics SDG 3 - Good Health and Well-being

URI

http://www.scopus.com/inward/record.url?scp=33744503690&partnerID=8YFLogxK

DOI

10.1107/S1744309105035670

Coleções

FCT: DQ - Artigos em revista internacional com arbitragem científica

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