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Siderophore-Mediated Iron Transport: Crystal Structure of FhuA with Bound Lipopolysaccharide
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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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“Given their overall structural ( Ferguson et al., 1998 ; Locher et al., 1998 ; Buchanan et al., 1999 ; Ferguson et al., 2002 ; Chimento et al., 2003 ; Cobessi et al., 2005a , b ; Buchanan et al., 2007 ; Cobessi et al., 2010 ; Grinter and Lithgow, 2019a , b ; Grinter and Lithgow, 2020 ) and sequence ( Klebba et al., 2021 ) commonalities, other LGPs likely internalize metal complexes, including Troj”
From Specificity and mechanism of TonB-dependent ferric catecholate uptake by Fiu (2024) · cites this paper as Ferguson et al., 1998
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Chami, M., Guilvout, I., Gregorini, M., Remigy, H., Müller, S. A., Valerio‐Lepiniec, M., Engel, A. H., Pugsley, A. P., & Bayan, N. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504463200 · Cited by 151
Metadata
- Authors
- Ferguson, A. D., Hofmann, E., Coulton, J. W., Diederichs, K., & Welte, W.
- Affiliations
- University of Konstanz (DE)
- Corresponding author
- Welte, Wolfram
- Venue
- Science
- Published
- 1998-12-18
- Volume
- 282
- Issue
- 5397
- Pages
- 2215-2220
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- 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
- green
- nbn-resolving.de
- 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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