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J. Biol. Chem., Vol. 282, Issue 52, 37717-37729, December 28, 2007

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The Structure of a Full-length Response Regulator from Mycobacterium tuberculosis in a Stabilized Three-dimensional Domain-swapped, Activated State^*

Jack King-Scott, Elzbieta Nowak¹, Efstratios Mylonas, Santosh Panjikar, Manfred Roessle, Dmitri I. Svergun, and Paul A. Tucker²

From the EMBL-Hamburg Outstation, c/o DESY, Notkestrasse 85, D-22603 Hamburg, Germany and the Institute of Crystallography, Russian Academy of Sciences, Leninsky pr. 59, Moscow 117333, Russia

The full-length, two-domain response regulator RegX3 from Mycobacterium tuberculosis is a dimer stabilized by three-dimensional domain swapping. Dimerization is known to occur in the OmpR/PhoB subfamily of response regulators upon activation but has previously only been structurally characterized for isolated receiver domains. The RegX3 dimer has a bipartite intermolecular interface, which buries 2357 Ų per monomer. The two parts of the interface are between the two receiver domains (dimerization interface) and between a composite receiver domain and the effector domain of the second molecule (interdomain interface). The structure provides support for the importance of threonine and tyrosine residues in the signal transduction mechanism. These residues occur in an active-like conformation stabilized by lanthanum ions. In solution, RegX3 exists as both a monomer and a dimer in a concentration-dependent equilibrium. The dimer in solution differs from the active form observed in the crystal, resembling instead the model of the inactive full-length response regulator PhoB.

Received for publication, June 20, 2007 , and in revised form, September 26, 2007.

The atomic coordinates and structure factors (code 2OQR) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* This work was supported by the Bundesministerium für Bildung und Forschung (German Science Ministry)-funded X-MTB consortium. 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.

¹ Present address: Argonne National Laboratory, 9700 S. Cass Ave., Argonne, IL 60439.

² To whom correspondence should be addressed. Tel.: 49-40-89901129; Fax: 49-40-89902149; E-mail: tucker{at}embl-hamburg.de.

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