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J. Biol. Chem., Vol. 281, Issue 30, 21399-21409, July 28, 2006

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NMR Structure of AbhN and Comparison with AbrBN

FIRST INSIGHTS INTO THE DNA BINDING PROMISCUITY AND SPECIFICITY OF AbrB-LIKE TRANSITION STATE REGULATOR PROTEINS^*

Benjamin G. Bobay, Geoffrey A. Mueller, Richele J. Thompson, Alexey G. Murzin^¶, Ronald A. Venters^||, Mark A. Strauch^**, and John Cavanagh¹

From the Department of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, North Carolina 27695, the Laboratory of Structural Biology, NIEHS, National Institutes of Health, Research Triangle Park, North Carolina 27709, ^¶Medical Research Council Centre for Protein Engineering, Hills Road, Cambridge CB2 2QH, United Kingdom, the ^||Duke University NMR Center, Durham, North Carolina 27710, and the^** Biomedical Sciences Department, Dental School, University of Maryland, Baltimore, Maryland 21201

Understanding the molecular mechanisms of transition state regulator proteins is critical, since they play a pivotal role in the ability of bacteria to cope with changing environments. Although much effort has focused on their genetic characterization, little is known about their structural and functional conservation. Here we present the high resolution NMR solution structure of the N-terminal domain of the Bacillus subtilis transition state regulator Abh (AbhN), only the second such structure to date. We then compare AbhN to the N-terminal DNA-binding domain of B. subtilis AbrB (AbrBN). This is the first such comparison between two AbrB-like transition state regulators. AbhN and AbrBN are very similar, suggesting a common structural basis for their DNA binding. However, we also note subtle variances between the AbhN and AbrBN structures, which may play important roles in DNA target specificity. The results of accompanying in vitro DNA-binding studies serve to highlight binding differences between the two proteins.

Received for publication, March 1, 2006 , and in revised form, April 4, 2006.

The atomic coordinates and structure factors (code 2FY9) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

The AbhN atomic coordinates have been deposited in the BioMagResBank (6826).

^* This work was supported in part by National Institutes of Health (NIH) Grants GM55769 (to J. C.) and GM46700 (to M. A. S.), a grant from the Kenan Institute for Engineering, Technology and Science (to J. C.) and the Intramural Research Program of NIEHS, NIH. 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: Dept. of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, NC 27695. Tel.: 919-513-4349; Fax: 919-515-2047; E-mail: john_cavanagh{at}ncsu.edu.

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