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

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Shabir NajmudinJosé A M Prates

Abstract

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 P4(3)2(1)2, containing a single molecule in the asymmetric unit. Native and seleno-L-methionine-derivative crystals diffracted to 2.1 and 2.8 A, respectively.

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Citations

Jan 21, 2009·Functional & Integrative Genomics·Mally Dori-BachashShmuel Pietrokovski
Dec 12, 2012·The Journal of Biological Chemistry·Ana S LuísHarry J Gilbert
Apr 21, 2011·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Ana S LuísShabir Najmudin
Jul 29, 2011·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Joana L A BrásShabir Najmudin
Oct 26, 2012·Biotechnology for Biofuels·Sarah MoraïsEdward A Bayer
Nov 30, 2005·The Journal of Biological Chemistry·Shabir NajmudinCarlos M G A Fontes

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