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J. Biol. Chem., Vol. 279, Issue 53, 55985-55994, December 31, 2004

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Structural Insights into the Mechanism of Formation of Cellulosomes Probed by Small Angle X-ray Scattering^*

Michal Hammel, Henri-Pierre Fierobe¶, Mirjam Czjzek, Stéphanie Finet||, and Véronique Receveur-Bréchot**

From the Architecture et Fonction des Macromolécules Biologiques, UMR 6098, CNRS and Universités d'Aix-Marseille I and II, 31 Chemin Joseph Aiguier, F-13402 Marseille cedex 20, France, ^¶Bioénergétique et Ingénierie des Protéines UPR9036, CNRS, 31 Chemin Joseph Aiguier, F-13402 Marseille cedex 20, France, Institute of Biophysics and X-ray Structure Research of the Austrian Academy of Sciences, Schmiedlstrasse 6, A-8042 Graz, Austria, and ^||ESRF, 6 rue Jules Horowitz, BP 220, F-38043 Grenoble cedex 9, France

Exploring the mechanism by which the multiprotein 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 Clostridium thermocellum and Clostridium 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.

Received for publication, August 5, 2004 , and in revised form, October 19, 2004.

^* This work was supported by the Centre National de la Recherche Scientifique, the Conseil Général des Bouches du Rhône, the Région Provence-Alpes-Côte d'Azur, and the Fonds zur Förderung der Wissenschaftlichen Forschung Grant J2220-N03 (to M. H.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^** To whom correspondence should be addressed. Tel.: 33-4-91-16-45-15; Fax: 33-4-91-16-45-36; E-mail: receveur{at}afmb.cnrs-mrs.fr.

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