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Structural Basis of Gating by the Outer Membrane Transporter FecA
Andrew D. Ferguson,1Ranjan Chakraborty,23Barbara S. Smith,1Lothar Esser,14Dick van der Helm,25Johann Deisenhofer1*
Siderophore-mediated acquisition systems facilitate iron uptake. We
present the crystallographic structure of the integralouter membrane
receptor FecA from Escherichia coli with and withoutferric
citrate at 2.5 and 2.0 angstrom resolution. FecA is composedof three
distinct domains: the barrel, plug, and NH2-terminalextension. Binding of ferric citrate triggers a conformationalchange
of the extracellular loops that close the external pocketof FecA.
Ligand-induced allosteric transitions are propagatedthrough the outer
membrane by the plug domain, signaling the occupancyof the receptor in
the periplasm. These data establish the structuralbasis of gating for
receptors dependent on the cytoplasmic membraneprotein 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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PERSPECTIVES
Kathleen Postle (1 March 2001) Science295 (5560), 1658.
[DOI: 10.1126/science.1070129] |Summary »|Full Text »|PDF »
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