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M408979200v1
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Papers In Press, published online ahead of print October 23, 2004
J. Biol. Chem, 10.1074/jbc.M408979200
Submitted on August 5, 2004
Revised on October 19, 2004
Accepted on October 23, 2004

Structural insights into the mechanism of formation of cellulosomes probed by small angle X-ray scattering

Michal Hammel, Henri-Pierre Fierobe, Mirjam Czjzek, Stephanie Finet, and Veronique Receveur-Brechot

AFMB, CNRS, Marseille, Cedex 20 13402

Corresponding Author: receveur{at}afmb.cnrs-mrs.fr

Exploring the mechanism by which the multi-protein complexes of cellulolytic organisms, the cellulosomes, attain their exceptional synergy is a challenge for biologists. We have studied the solution structures of the Clostridium cellulolyticum cellulosomal enzyme Cel48F in the free and complexed states with cohesins from C. thermocellum and C. cellulolyticum by small angle X-ray scattering, in order to investigate the conformational events likely to occur upon complexation. The solution structure of the free cellulase indicates that the dockerin module is folded whereas the linker connecting the catalytic module to the dockerin is extended and flexible. Remarkably, the docking of the different cohesins onto Cel48F leads to a pleating of the linker. The global structure determined here allowed modeling of the atomic structure of the C. cellulolyticum dockerin/cohesin interface, highlighting the local differences between both organisms responsible for the species specificity.


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