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Science 18 December 1998:
Vol. 282. no. 5397, pp. 2215 - 2220
DOI: 10.1126/science.282.5397.2215
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Research Articles

Siderophore-Mediated Iron Transport: Crystal Structure of FhuA with Bound Lipopolysaccharide

Andrew D. Ferguson, Eckhard Hofmann, James W. Coulton, Kay Diederichs, Wolfram Welte *

FhuA, the receptor for ferrichrome-iron in Escherichia coli, is a member of a family of integral outer membrane proteins, which, together with the energy-transducing protein TonB, mediate the active transport of ferric siderophores across the outer membrane of Gram-negative bacteria. The three-dimensional structure of FhuA is presented here in two conformations: with and without ferrichrome-iron at resolutions of 2.7 and 2.5 angstroms, respectively. FhuA is a beta  barrel composed of 22 antiparallel beta  strands. In contrast to the typical trimeric arrangement found in porins, FhuA is monomeric. Located within the beta  barrel is a structurally distinct domain, the "cork," which mainly consists of a four-stranded beta  sheet and four short alpha  helices. A single lipopolysaccharide molecule is noncovalently associated with the membrane-embedded region of the protein. Upon binding of ferrichrome-iron, conformational changes are transduced to the periplasmic pocket of FhuA, signaling the ligand-loaded status of the receptor. Sequence homologies and mutagenesis data are used to propose a structural mechanism for TonB-dependent siderophore-mediated transport across the outer membrane.

A. D. Ferguson is in the Department of Microbiology and Immunology, McGill University, 3775 University Street, Montreal, Quebec, Canada H3A 2B4, and Fakultät für Biologie, Universität Konstanz, M656, Konstanz, Germany D-78457. E. Hofmann, K. Diederichs, and W. Welte are in the Fakultät für Biologie, Universität Konstanz, M656, Konstanz, Germany D-78457. J. W. Coulton is in the Department of Microbiology and Immunology, McGill University, 3775 University Street, Montreal, Quebec, Canada H3A 2B4.
*   To whom correspondence should be addressed. E-mail: wolfram.welte{at}uni-konstanz.de

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Interactions between the Outer Membrane Ferric Citrate Transporter FecA and TonB: Studies of the FecA TonB Box.
M. Ogierman and V. Braun (2003)
J. Bacteriol. 185, 1870-1885
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Analysis of Residues Determining Specificity of Vibrio cholerae TonB1 for Its Receptors.
A. R. Mey and S. M. Payne (2003)
J. Bacteriol. 185, 1195-1207
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