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Originally published In Press as doi:10.1074/jbc.M100195200 on February 13, 2001

J. Biol. Chem., Vol. 276, Issue 20, 17373-17379, May 18, 2001
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The FadR·DNA Complex
TRANSCRIPTIONAL CONTROL OF FATTY ACID METABOLISM IN ESCHERICHIA COLI*

Yibin XuDagger , Richard J. Heath§, Zhenmei LiDagger , Charles O. Rock§, and Stephen W. WhiteDagger ||

From the Departments of Dagger  Structural Biology and § Biochemistry, St Jude Children's Research Hospital, Memphis, Tennessee 38105 and the  Department of Molecular Sciences, University of Tennessee Health Science Center, Memphis, Tennessee 38163

In Escherichia coli, the expression of fatty acid metabolic genes is controlled by the transcription factor, FadR. The affinity of FadR for DNA is controlled by long chain acyl-CoA molecules, which bind to the protein and modulate gene expression. The crystal structure of FadR reveals a two domain dimeric molecule where the N-terminal domains bind DNA, and the C-terminal domains bind acyl-CoA. The DNA binding domain has a winged-helix motif, and the C-terminal domain resembles the sensor domain of the Tet repressor. The FadR·DNA complex reveals how the protein interacts with DNA and specifically recognizes a palindromic sequence. Structural and functional similarities to the Tet repressor and the BmrR transcription factors suggest how the binding of the acyl-CoA effector molecule to the C-terminal domain may affect the DNA binding affinity of the N-terminal domain. We suggest that the binding of acyl-CoA disrupts a buried network of charged and polar residues in the C-terminal domain, and the resulting conformational change is transmitted to the N-terminal domain via a domain-spanning alpha -helix.

* This work was supported by National Institutes of Health Grant GM34496 (to C. O. R.), Cancer Center (CORE) Support Grant CA 21765, and the American Lebanese Syrian Associated Charities (ALSAC).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 1HW1 and 1HW2) 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: Dept. of Structural Biology, St Jude Children's Research Hospital, 332 N. Lauderdale, Memphis, TN 38105-2794. Tel.: 901-495-3040; Fax: 901-495-3032; E-mail: stephen.white@stjude.org.

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