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Originally published In Press as doi:10.1074/jbc.M105819200 on October 1, 2001

J. Biol. Chem., Vol. 276, Issue 50, 47178-47184, December 14, 2001
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Crystal Structure of MtaN, a Global Multidrug Transporter Gene Activator*

Michael H. GodseyDagger , Natalya N. Baranova§, Alexander A. Neyfakh§, and Richard G. BrennanDagger

From the Dagger  Department of Biochemistry and Molecular Biology, Oregon Health & Science University, Portland, Oregon 97201-3098 and the § Center for Pharmaceutical Biotechnology, University of Illinois, Chicago, Illinois 60607

MtaN (Multidrug Transporter Activation, N terminus) is a constitutive, transcriptionally active 109-residue truncation mutant, which contains only the N-terminal DNA-binding and dimerization domains of MerR family member Mta. The 2.75 Å resolution crystal structure of apo-MtaN reveals a winged helix-turn-helix protein with a protruding 8-turn helix (alpha 5) that is involved in dimerization by the formation of an antiparallel coiled-coil. The hydrophobic core and helices alpha 1 through alpha 4 are structurally homologous to MerR family member BmrR bound to DNA, whereas one wing (Wing 1) is shifted. Differences between the orientation of alpha 5 with respect to the core and the revolution of the antiparallel coiled-coil lead to significantly altered conformations of MtaN and BmrR dimers. These shifts result in a conformation of MtaN that appears to be incompatible with the transcription activation mechanism of BmrR and suggest that additional DNA-induced structural changes are necessary.

* This work was supported by National Institutes of Health Grant AI 48593 (to R. G. B.) and Training Grant GM08617-05 (to M. H. G.), National Science Foundation Grant MCB-9816983 (to A. A. N.), and the N. L. Tartar Trust.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

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

To whom correspondence should be addressed. Tel.: 503-494-4427; Fax: 503-494-8393; E-mail: brennanr@ohsu.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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