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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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Citations
Cites
MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
Kraulis, P. J. (1991) · Journal of Applied Crystallography · doi:10.1107/s0021889891004399 · Cited by 14,011
Jones, T. A., Zou, J.-Y., Cowan, S. W., & Kjeldgaard, M. (1991) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767390010224 · Cited by 12,616
Protein Structure Comparison by Alignment of Distance Matrices
Holm, L., & Sander, C. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1489 · Cited by 3,984
Free R value: a novel statistical quantity for assessing the accuracy of crystal structures
Brünger, A. T. (1992) · Nature · doi:10.1038/355472a0 · Cited by 3,877
[26] Raster3D: Photorealistic molecular graphics
Merritt, E. A., & Bacon, D. (1997) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(97)77028-9 · Cited by 3,749
Cation-π Interactions in Chemistry and Biology: A New View of Benzene, Phe, Tyr, and Trp
Dougherty, D. A. (1996) · Science · doi:10.1126/science.271.5246.163 · Cited by 2,658
Fortelle, E. D. L., & Bricogne, G. (1997) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(97)76073-7 · Cited by 1,892
Escherichia coli and Salmonella.
Neidhart, F. C. (1996) · Cited by 1,577
Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector
Kabsch, W. (1988) · Journal of Applied Crystallography · doi:10.1107/s0021889888007903 · Cited by 1,501
Determination of Macromolecular Structures from Anomalous Diffraction of Synchrotron Radiation
Hendrickson, W. A. (1991) · Science · doi:10.1126/science.1925561 · Cited by 1,131
Flagged first, then by citations
Research works printed but not linked: 6
- 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.
- 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;
- Letain T. E., Postle K., ibid. 24, 271 (1997) .
- G. Adam and M. Delbrück in Structural Chemistry and Molecular Biology A. Rich and N. Davidson Eds. (Freeman San Francisco 1968) pp. 198–215.
- Terwilliger T. C., Berendzen J., Acta Crystallogr. D53, 571 (1997);
- Cowtan K., Acta Crystallogr. D50, 760 (1994);
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Items 501–600 of 786
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Fardeau, S., Audic, N., & Sasaki, A. (2011) · Cited by 20
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Azevedo, M., Sousa, A., de Sousa, J. A. M., Thompson, J. A., Proença, J. T., & Gordo, I. (2016) · PLoS ONE · doi:10.1371/journal.pone.0146123 · Cited by 20
An 8-Å Projected Structure of FhuA, A “Ligand-Gated” Channel of the Escherichia coli Outer Membrane
Lambert, O., Moeck, G., Lévy, D., Plançon, L., Letellìer, L., & Rigaud, J. L. (1999) · Journal of Structural Biology · doi:10.1006/jsbi.1999.4115 · Cited by 20
Shen, J.-S., Geoffroy, V., Neshat, S., Jia, Z., Meldrum, A., Meyer, J., & Poole, K. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.24.8511-8515.2005 · Cited by 20
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Braun, V., & Hantke, K. (2013) · Springer briefs in molecular science · doi:10.1007/978-94-007-6088-2_2 · Cited by 18
Global redesign of a native β-barrel scaffold
Wolfe, A. J., Mohammad, M. M., Thakur, A. K., & Movileanu, L. (2015) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2015.10.006 · Cited by 19
Residue K556‐A Light Triggerable Gatekeeper to Sterically Control Translocation in FhuA
Güven, A., Dworeck, T., Fioroni, M., & Schwaneberg, U. (2011) · Advanced Engineering Materials · doi:10.1002/adem.201080127 · Cited by 19
James, K. J., Hancock, M. A., Moreau, V., Molina, F., & Coulton, J. W. (2008) · Protein Science · doi:10.1110/ps.036244.108 · Cited by 20
Self-citationChiral separation of d / l -arginine with whole cells through an engineered FhuA nanochannel
Anand, D., Dhoke, G. V., Gehrmann, J., Garakani, T. M., Davari, M. D., Bocola, M., Zhu, L., & Schwaneberg, U. (2019) · Chemical Communications · doi:10.1039/c9cc00154a · Cited by 19
Khan, A. G., Shouldice, S. R., Tari, L. W., & Schryvers, A. B. (2007) · Biochemical Journal · doi:10.1042/bj20061589 · Cited by 19
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Smallwood, C., Jordan, L. D., Trinh, V., Schürch, D., Gala, A., Hanson, M., Shipelskiy, Y., Majumdar, A., Newton, S. M. C., & Klebba, P. E. (2014) · The Journal of General Physiology · doi:10.1085/jgp.20131115907012014c · Cited by 19
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Harms, N., Oudhuis, W. C., Eppens, E. A., Valent, Q. A., Koster, M. C., Luirink, J., & Oudega, B. (1999) · PubMed · Cited by 19
Matzanke, B. F. (2005) · Wiley eBooks · doi:10.1002/0470862106.ia117 · Cited by 19
Wing, H. J., Goldman, S. R., Ally, S., & Goldberg, M. B. (2005) · Infection and Immunity · doi:10.1128/iai.73.2.1217-1220.2005 · Cited by 18
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Maier, E., Polleichtner, G., Boeck, B., Schinzel, R., & Benz, R. (2001) · Journal of Bacteriology · doi:10.1128/jb.183.2.800-803.2001 · Cited by 18
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Law, C. J., Penfold, C. N., Walker, D. C., Moore, G. R., James, R., & Kleanthous, C. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00511-8 · Cited by 18
Olshvang, E., Szebesczyk, A., Kozłowski, H., Hadar, Y., Gumienna‐Kontecka, E., & Shanzer, A. (2015) · Dalton Transactions · doi:10.1039/c5dt02685g · Cited by 19
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Zakharov, S. D., Wang, X. S., & Cramer, W. A. (2016) · Biochemistry · doi:10.1021/acs.biochem.6b00621 · Cited by 17
Pristovšek, P., Simčič, S., Wraber, B., & Urleb, U. (2005) · Journal of Medicinal Chemistry · doi:10.1021/jm050762a · Cited by 17
Shi, R., Pineda, M., Ajamian, E., Cui, Q., Matte, A., & Cygler, M. (2008) · Journal of Bacteriology · doi:10.1128/jb.01049-08 · Cited by 17
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Jackups, R., & Liang, J. (2008) · IEEE Transactions on Computational Biology and Bioinformatics · doi:10.1109/tcbb.2008.101 · Cited by 17
Reyes-Cortés, R., Martínez-Peñafiel, E., Martínez‐Pérez, F., de la Garza, M., & Kameyama, L. (2012) · Microbiology · doi:10.1099/mic.0.060970-0 · Cited by 17
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Zampara, A., Sørensen, M. C. H., Grimon, D., Antenucci, F., Briers, Y., & Brøndsted, L. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/408948 · Cited by 17
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Udho, E., Jakes, K. S., & Finkelstein, A. (2012) · Biochemistry · doi:10.1021/bi300493u · Cited by 17
Lantez, V., Nikolaidis, I., Rechenmann, M., Vernet, T., & Noirclerc‐Savoye, M. (2014) · Engineering in Life Sciences · doi:10.1002/elsc.201400187 · Cited by 16
Garakani, T. M., Liu, Z., Glebe, U., Gehrmann, J., Lazar, J., Mertens, M. A. S., Möller, M., Hamzelui, N., Zhu, L., Schnakenberg, U., et al. (2019) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.9b09302 · Cited by 16
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Jiménez-Vega, F., & Vargas‐Albores, F. (2007) · Journal of Shellfish Research · doi:10.2983/0730-8000(2007)26[1169:iolvaa]2.0.co;2 · Cited by 16
Banerjee, S., Siburt, C. J. P., Mistry, S., Noto, J. M., DeArmond, P. D., Fitzgerald, M. C., Lambert, L. A., Cornelissen, C. N., & Crumbliss, A. L. (2012) · Metallomics · doi:10.1039/c2mt20037f · Cited by 16
Tomita, N., Mohammad, M. M., Niedzwiecki, D. J., Ohta, M., & Movileanu, L. (2012) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2012.12.003 · Cited by 16
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Braun, V., Mahren, S., & Sauter, A. (2005) · BioMetals · doi:10.1007/s10534-005-3497-0 · Cited by 17
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Hu, W., & Zheng, H. (2021) · Communications Biology · doi:10.1038/s42003-021-02916-2 · Cited by 17
de Rossi, B. P., Friedman, L. E., Belzoni, C. B., Savino, S., Aricò, B., Rappuoli, R., Masignani, V., & Franco, M. A. (2003) · Research in Microbiology · doi:10.1016/s0923-2508(03)00115-3 · Cited by 15
Graham, M., & Lo, R. Y. C. (2002) · Veterinary Microbiology · doi:10.1016/s0378-1135(01)00415-1 · Cited by 15
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Wolfe, A. J., Hsueh, Y.-C., Blanden, A. R., Mohammad, M. M., Pham, B., Thakur, A. K., Loh, S. N., Chen, M., & Movileanu, L. (2017) · Analytical Chemistry · doi:10.1021/acs.analchem.7b01339 · Cited by 15
Charbit, A., Andersen, C., Jiang, W., Schiffler, B., Michel, V., Benz, R., & Hofnung, M. J. (2000) · Molecular Microbiology · doi:10.1046/j.1365-2958.2000.01748.x · Cited by 15
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Braun, V., Hartmann, M. D., & Hantke, K. (2022) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuac010 · Cited by 17
Guo, J.-X., Wood, S. J., David, S. A., & Lushington, G. H. (2005) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2005.10.025 · Cited by 14
TRZASKA, S. M., Toone, E. J., & Crumbliss, A. L. (2000) · Inorganic Chemistry · doi:10.1021/ic9908571 · Cited by 14
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Zhang, X. C., & Han, L. (2016) · Protein & Cell · doi:10.1007/s13238-016-0273-6 · Cited by 13
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Sansom, M. S. P. (1999) · Current Biology · doi:10.1016/s0960-9822(99)80157-2 · Cited by 13
Olczak, T. (2006) · Archives of Microbiology · doi:10.1007/s00203-006-0151-3 · Cited by 13
Wirgau, J. I., & Crumbliss, A. L. (2003) · Inorganic Chemistry · doi:10.1021/ic034157e · Cited by 13
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Oakhill, J. S., Joannou, C. L., Buchanan, S. K., GORRINGE, A. R., & Evans, R. W. (2002) · Biochemical Journal · doi:10.1042/bj20020500 · Cited by 13
Sims, K. L., & Schryvers, A. B. (2003) · Journal of Bacteriology · doi:10.1128/jb.185.8.2603-2610.2003 · Cited by 13
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Alteri, C., Teri, A., Liporace, M. F., Muscatello, A., Terranova, L., Schianca, M. C., Salari, F., Orena, B. S., Silverj, F. G., Bernazzani, M., et al. (2024) · Annals of Clinical Microbiology and Antimicrobials · doi:10.1186/s12941-024-00763-7 · Cited by 12
Pawelek, P. D., & Coulton, J. W. (2004) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2004.06.002 · Cited by 12
Self-citationZhai, L., Xie, J., Feng, H., Sun, S., Cheng, K., & Yao, S. (2020) · Extremophiles · doi:10.1007/s00792-020-01209-6 · Cited by 12
Pocanschi, C. L., & Kleinschmidt, J. H. (2022) · The Journal of Membrane Biology · doi:10.1007/s00232-022-00238-w · Cited by 12
Brillet, K., Meksem, A., Lauber, E., Reimmann, C., & Cobessi, D. (2009) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909002200 · Cited by 14
Cristalli, G., Dirusso, C., & Black, P. N. (2000) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2000.1794 · Cited by 12
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Rodríguez-Ropero, F., & Fioroni, M. (2012) · Journal of Structural Biology · doi:10.1016/j.jsb.2011.12.021 · Cited by 11
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Rocco, M. A., Kim, J., Burns, A., Kostecki, J., Doody, A. M., Wiesner, U. B., & DeLisa, M. P. (2009) · Bioconjugate Chemistry · doi:10.1021/bc9000118 · Cited by 11
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Kinzel, J., Sauer, D. F., Bocola, M., Arlt, M., Garakani, T. M., Thiel, A., Beckerle, K., Polen, T., Okuda, J., & Schwaneberg, U. (2017) · Beilstein Journal of Organic Chemistry · doi:10.3762/bjoc.13.148 · Cited by 11
Ensari, Y., Santos, G. D. A., Ruff, A. J., & Schwaneberg, U. (2020) · Enzyme and Microbial Technology · doi:10.1016/j.enzmictec.2020.109555 · Cited by 11
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Braun, V., & Hantke, K. (2007) · Springer eBooks · doi:10.1007/7171_2006_078 · Cited by 11
Spasojević, I., & Crumbliss, A. L. (1999) · Inorganic Chemistry · doi:10.1021/ic9813664 · Cited by 11
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Braun, V., Braun, M., & Killmann, H. (2005) · Kluwer Academic Publishers eBooks · doi:10.1007/0-306-46840-9_4 · Cited by 11
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Tomitake Tsukihara, A., & Lee, S. J. (1999) · Journal of Synchrotron Radiation · doi:10.1107/s0909049599006184 · Cited by 11
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Gromiha, M. M., Yabuki, Y., & Suwa, M. (2007) · Journal of Chemical Information and Modeling · doi:10.1021/ci700222s · Cited by 10
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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
- 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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