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Architecture of a protein central to iron homeostasis: crystal structure and spectroscopic analysis of the ferric uptake regulator
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Summary: Iron is an essential element for almost all organisms, although an overload of this element results in toxicity because of the formation of hydroxyl radicals. Consequently, most living entities have developed sophisticated mechanisms to control their intracellular iron concentration. In many bacteria, including the opportunistic pathogen Pseudomonas aeruginosa , this task is performed by the ferric uptake regulator (Fur). Fur controls a wide variety of basic physiological processes including iron uptake systems and the expression of exotoxin A. Here, we present the first crystal structure of Fur from P. aeruginosa in complex with Zn 2+ determined at a resolution of 1.8 Å. Furthermore, X‐ray absorption spectroscopic measurements and microPIXE analysis were performed in order to characterize the distinct zinc and iron binding sites in solution. The combination of these complementary techniques enables us to present a model for the activation and DNA binding of the Fur protein.
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“Zinc ions were used in all previous Fur structures 7 , 14 , 15 , 16 , 17 .”
From Mechanistic insights into metal ion activation and operator recognition by the ferric uptake regulator (2015) · cites this paper as [7]
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Cavazza, C., Collin‐Faure, V., Pérard, J., Diemer, H., Cianférani, S., Rabilloud, T., & Darrouzet, É. (2021) · Journal of Proteomics · doi:10.1016/j.jprot.2021.104389 · Cited by 16
de Lorenzo, V., Pérez‐Martín, J., Escolar, L., Pesole, G., & Bertoni, G. (2014) · ASM Press eBooks · doi:10.1128/9781555816544.ch13 · Cited by 15
Mechanisms and Regulation of Iron Uptake in the Rhizobia
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Boyd, J. M., Ryan Kaler, K., Esquilín-Lebrón, K., Pall, A., Campbell, C. J., Foley, M. E., Rios-Delgado, G., Mustor, E. M., Stephens, T. G., Bovermann, H., et al. (2024) · mBio · doi:10.1128/mbio.02310-24 · Cited by 14
Metadata
- Authors
- Pohl, E., Haller, J. C., Mijovilovich, A., Meyer‐Klaucke, W., Garman, E., & Vasil, M. L.
- Affiliations
- European Molecular Biology Laboratory (DE)
- University of Oxford (GB)
- Corresponding author
- Pohl, Ehmke
- Venue
- Molecular Microbiology
- Publisher
- Wiley
- Published
- 2003-02
- Volume
- 47
- Issue
- 4
- Pages
- 903-915
- ISSN
- 0950-382X (ISSN-L)
- 1365-2958
- OpenAlex
- W2098798603
- Cited by
- 326
- References
- 62
- Citations by year
- 2026: 4 · 2025: 6 · 2024: 8 · 2023: 8 · 2022: 8 · 2021: 6 · 2020: 11 · 2019: 13 · 2018: 9 · 2017: 16 · 2016: 10 · 2015: 10 · 2014: 20 · 2013: 14 · 2012: 23
- FWCI
- 15.04
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Molecular Microbiology (publishedVersion)
- PubMed (publishedVersion)
- Durham Research Online (Durham University) (acceptedVersion)
- DESY Publication Database (PUBDB) (Deutsches Elektronen-Synchrotron) (submittedVersion)
- Durham Research Online (Durham University) (submittedVersion)
- Durham Research Online (Durham University) (submittedVersion, cc-by)
- Funders
- National Institutes of Health
- National Institute of Allergy and Infectious Diseases (AI-15490)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Keywords
- ferric uptake regulator, Fur protein, Pseudomonas aeruginosa, iron homeostasis, zinc binding, iron binding, protein crystal structure, DNA binding, transcriptional regulation, exotoxin A, X-ray absorption spectroscopy
- MeSH terms
- Amino Acid Sequence, Bacterial Proteins, DNA, Bacterial, Homeostasis, Iron, Models, Molecular, Molecular Sequence Data, Protein Conformation, Pseudomonas aeruginosa, Repressor Proteins, Spectrometry, X-Ray Emission, Spectrum Analysis, X-Rays, Molecular Structure, Sequence Homology, Amino Acid, Crystallography, X-Ray, Macromolecular Substances, Static Electricity
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