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J. Biol. Chem., Vol. 280, Issue 15, 14780-14789, April 15, 2005

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Activation of the LicT Transcriptional Antiterminator Involves a Domain Swing/Lock Mechanism Provoking Massive Structural Changes^*

Marc Graille, Cong-Zhao Zhou¶||, Véronique Receveur-Bréchot**, Bruno Collinet¶, Nathalie Declerck, and Herman van Tilbeurgh¶¶

From the Laboratoire d'Enzymologie et Biochimie Structurales, CNRS-UPR9063, Btiment 34, 1 Avenue de la Terrasse, 91198 Gif sur Yvette, France, the ^¶Institut de Biochimie et de Biophysique Moléculaire et Cellulaire, CNRS-UMR8619, Université Paris-Sud, Btiment 430, 91405 Orsay, France, ^**Architecture et Fonction des Macromolécules Biologiques, CNRS-UMR6098, Université d'Aix-Marseille I et II, 31 chemin Joseph Aiguier, 13402 Marseille CEDEX 20, France, the Centre de Biochimie structurale, CNRS-UMR9955Université de Montpellier I/INSERM U414, 29 rue de Navacelles, 34090 Montpellier, France, and Microbiologie et Génétique Moléculaire, CNRS/INRA/INA-PG UMR2585, 78850 Thiverval Grignon, France

The transcriptional antiterminator protein LicT regulates the expression of Bacillus subtilis operons involved in -glucoside metabolism. It consists of an N-terminal RNA-binding domain (co-antiterminator (CAT)) and two phosphorylatable phosphotransferase system regulation domains (PRD1 and PRD2). In the activated state, each PRD forms a dimeric unit with the phosphorylation sites totally buried at the dimer interface. Here we present the 1.95 Å resolution structure of the inactive LicT PRDs as well as the molecular solution structure of the full-length protein deduced from small angle x-ray scattering. Comparison of native (inactive) and mutant (constitutively active) PRD crystal structures shows massive tertiary and quaternary rearrangements of the entire regulatory domain. In the inactive state, a wide swing movement of PRD2 results in dimer opening and brings the phosphorylation sites to the protein surface. This movement is accompanied by additional structural rearrangements of both the PRD1-PRD1 ' interface and the CAT-PRD1 linker. Small angle x-ray scattering experiments indicate that the amplitude of the PRD2 swing might even be wider in solution than in the crystals. Our results suggest that PRD2 is highly mobile in the native protein, whereas it is locked upon activation by phosphorylation.

Received for publication, December 29, 2004 , and in revised form, January 28, 2005.

^* This work was supported by grants from the Ministère de la Recherche et de la Technologie (Programme Génopoles) and the Association pour la Recherche contre le Cancer (to M. G.). 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.

The on-line version of this article (available at http://www.jbc.org) contains a supplemental figure.

The atomic coordinates and structure factors (code 1TLV) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

Both authors contributed equally to this work.

^|| Present address: School of Life Science, University of Science and Technology of China, Hefei Anhui, 230027, China.

^¶¶ To whom correspondence should be addressed. Tel.: 33-1-69-15-31-55; Fax: 33-1-69-85-37-15; E-mail: Herman.Van-Tilbeurgh{at}ibbmc.u-psud.fr.

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