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

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Ferguson, Andrew D., Hofmann, Eckhard, Coulton, James W., Diederichs, Kay, Welte, Wolfram·1998·Science
DOI 10.1126/science.282.5397.2215
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Abstract

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.

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Research works printed but not linked: 6

  1. V. Braun K. Hantke W. Köster in Metal Ions in Biological Systems A. Sigel and H. Sigel Eds. (Marcel Dekker New York 1998) pp. 67–145.
  2. W. Welte et al. in Proceedings of the NATO Advanced Workshop: New Methods for the Study of Molecular Aggregates K. Standing and W. Ens Eds. (Kluwer Academic Boston 1998) pp. 239–276;
  3. Letain T. E., Postle K., ibid. 24, 271 (1997) .
  4. G. Adam and M. Delbrück in Structural Chemistry and Molecular Biology A. Rich and N. Davidson Eds. (Freeman San Francisco 1968) pp. 198–215.
  5. Terwilliger T. C., Berendzen J., Acta Crystallogr. D53, 571 (1997);
  6. Cowtan K., Acta Crystallogr. D50, 760 (1994);

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Metadata

Authors
Ferguson, A. D., Hofmann, E., Coulton, J. W., Diederichs, K., & Welte, W.
Affiliations
University of Konstanz (DE)
Corresponding author
Welte, Wolfram
ORCID
Venue
Science
Publisher
American Association for the Advancement of Science (AAAS)
Published
1998-12-18
Volume
282
Issue
5397
Pages
2215-2220
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
DOI
10.1126/science.282.5397.2215
OpenAlex
W2084608838
Cited by
787
References
45
Citations by year
2026: 7 · 2025: 9 · 2024: 15 · 2023: 10 · 2022: 10 · 2021: 17 · 2020: 13 · 2019: 14 · 2018: 16 · 2017: 21 · 2016: 19 · 2015: 12 · 2014: 22 · 2013: 24 · 2012: 27
FWCI
22.45
Type
journal article
Language
en
Open access
Licence
cc-by-nc-nd
Locations
  • Science (publishedVersion)
  • PubMed (publishedVersion)
  • KOPS (University of Konstanz) (submittedVersion, cc-by-nc-nd)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
  • Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
Keywords
FhuA, siderophore transport, TonB, outer membrane receptor, lipopolysaccharide binding, beta-barrel proteins, Escherichia coli, Gram-negative bacteria, iron acquisition, conformational change, TonB-dependent transport, protein crystal structure
MeSH terms
Bacterial Outer Membrane Proteins, Bacterial Proteins, Binding Sites, Biological Transport, Active, Cell Membrane, Diffusion, Escherichia coli, Ferric Compounds, Ferrichrome, Hydrogen Bonding, Ligands, Lipopolysaccharides, Membrane Proteins, Models, Molecular, Protein Conformation, Receptors, Virus, Signal Transduction, Protein Structure, Secondary, Crystallography, X-Ray, Escherichia coli Proteins

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