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Science 1 March 2002:
Vol. 295. no. 5560, pp. 1715 - 1719
DOI: 10.1126/science.1067313

Reports

Structural Basis of Gating by the Outer Membrane Transporter FecA

Andrew D. Ferguson,1 Ranjan Chakraborty,23 Barbara S. Smith,1 Lothar Esser,14 Dick van der Helm,25 Johann Deisenhofer1*

Siderophore-mediated acquisition systems facilitate iron uptake. We present the crystallographic structure of the integral outer membrane receptor FecA from Escherichia coli with and without ferric citrate at 2.5 and 2.0 angstrom resolution. FecA is composed of three distinct domains: the barrel, plug, and NH2-terminal extension. Binding of ferric citrate triggers a conformational change of the extracellular loops that close the external pocket of FecA. Ligand-induced allosteric transitions are propagated through the outer membrane by the plug domain, signaling the occupancy of the receptor in the periplasm. These data establish the structural basis of gating for receptors dependent on the cytoplasmic membrane protein TonB. By compiling available data for this family of receptors, we propose a mechanism for the energy-dependent transport of siderophores.

1 Howard Hughes Medical Institute and Department of Biochemistry, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390, USA.
2 Department of Chemistry and Biochemistry, University of Oklahoma, 620 Parrington Oval, Norman, OK 73019, USA.
3 Department of Health Sciences, College of Public and Allied Health, East Tennessee State University, Post Office Box 70673, Johnson City, TN 37614, USA.
4 Laboratory of Cell Biology, National Cancer Institute, National Institutes of Health, 37 Convent Drive, Bethesda, MD 20892, USA.
5 Department of Biochemistry and Microbiology, University of Victoria, Post Office Box 3055, Victoria, British Columbia V8W 3P6, Canada.
*   To whom correspondence should be addressed. E-mail: johann.deisenhofer{at}utsouthwestern.edu


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