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J. Biol. Chem., Vol. 281, Issue 14, 9659-9666, April 7, 2006

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The Structural Basis of Signal Transduction for the Response Regulator PrrA from Mycobacterium tuberculosis^*

From the European Molecular Biology Laboratory (EMBL), Hamburg Outstation, Notkestrasse 85, D-22603 Hamburg, Germany

The structure of the two-domain response regulator PrrA from Mycobacterium tuberculosis shows a compact structure in the crystal with a well defined interdomain interface. The interface, which does not include the interdomain linker, makes the recognition helix and the trans-activation loop of the effector domain inaccessible for interaction with DNA. Part of the interface involves hydrogen-bonding interactions of a tyrosine residue in the receiver domain that is believed to be involved in signal transduction, which, if disrupted, would destabilize the interdomain interface, allowing a more extended conformation of the molecule, which would in turn allow access to the recognition helix. In solution, there is evidence for an equilibrium between compact and extended forms of the protein that is far toward the compact form when the protein is inactivated but moves toward a more extended form when activated by the cognate sensor kinase PrrB.

Received for publication, November 8, 2005 , and in revised form, January 17, 2006.

The atomic coordinates and structure factors (code 1YS6 and 1YS7) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* 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 To whom correspondence should be addressed: EMBL Hamburg Outstation, c/o DESY, Notkestrasse 85, D-22603 Hamburg Germany. Tel.: 49-40-89902129; Fax: 49-40-89902149; E-mail: tucker{at}embl-hamburg.de.

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