Crystal structure of the Vibrio cholerae ferric uptake regulator (Fur) reveals insights into metal co‐ordination
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Summary: The ferric uptake regulator (Fur) is a metal‐dependent DNA‐binding protein that acts as both a repressor and an activator of numerous genes involved in maintaining iron homeostasis in bacteria. It has also been demonstrated in Vibrio cholerae that Fur plays an additional role in pathogenesis, opening up the potential of Fur as a drug target for cholera. Here we present the crystal structure of V. cholerae Fur that reveals a very different orientation of the DNA‐binding domains compared with that observed in Pseudomonas aeruginosa Fur. Each monomer of the dimeric Fur protein contains two metal binding sites occupied by zinc in the crystal structure. In the P. aeruginosa study these were designated as the regulatory site (Zn1) and structural site (Zn2). This V. cholerae Fur study, together with studies on Fur homologues and paralogues, suggests that in fact the Zn2 site is the regulatory iron binding site and the Zn1 site plays an auxiliary role. There is no evidence of metal binding to the cysteines that are conserved in many Fur homologues, including Escherichia coli Fur. An analysis of the metal binding properties shows that V. cholerae Fur can be activated by a range of divalent metals.
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Crystallographic studies of E. coli Fur and its homologs revealed that Fur proteins may exist as a homodimer or a tetramer, with each monomer containing three metal-binding sites: site 1 (coordinated by His-87, Asp-89, Glu-108, and His-125) located within the dimerization domain; site 2 (coordinated by His-33, Glu-81, His-88, and His-90) connects the DNA-binding domain and the dimerization domain;
“Crystallographic studies of E. coli Fur (10) and its homologs from other bacteria (11, 12, 13, 14, 15) revealed that Fur proteins may exist as a homodimer or a tetramer, with each monomer containing three metal-binding sites: site 1 (coordinated by His-87, Asp-89, Glu-108, and His-125) is located within the dimerization domain; site 2 (coordinated by His-33, Glu-81, His-88, and His-90) connects”
From Binding of a [2Fe–2S] cluster drives dimerization of ferric uptake regulator (Fur) in Escherichia coli (2025) · cites this paper as [12]
Split into 2 atoms — 0 confirmed, 1 partially supported, 1 disputed, 0 misattributed, 0 unverifiable. Expand the claim to see per-atom verdicts.
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Experimental — accuracy not yet measuredThe overall holo-Fur structure from MSR-1 was similar to that from other prokaryotes, for example r.m.s.d.=1.9 Å compared with Vibrio cholerae.
“The overall holo-Fur structure from MSR-1 was similar to that from other prokaryotes (for example, r.m.s.d.=1.9 Å compared with that from Vibrio cholerae ) 15 .”
From Mechanistic insights into metal ion activation and operator recognition by the ferric uptake regulator (2015) · cites this paper as [15]
Zinc ions were used in all previous Fur structures.
“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 [15]
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- Authors
- Sheikh, M. A., & Taylor, G. L.
- Affiliations
- University of St Andrews (GB)
- Corresponding author
- Taylor, Garry L.
- Venue
- Molecular Microbiology
- Publisher
- Wiley
- Published
- 2009-05-22
- Volume
- 72
- Issue
- 5
- Pages
- 1208-1220
- ISSN
- 0950-382X (ISSN-L)
- 1365-2958
- OpenAlex
- W2003090592
- Cited by
- 126
- References
- 51
- Citations by year
- 2026: 1 · 2025: 5 · 2024: 3 · 2023: 3 · 2022: 4 · 2021: 4 · 2020: 9 · 2019: 5 · 2018: 6 · 2017: 7 · 2016: 6 · 2015: 7 · 2014: 9 · 2013: 12 · 2012: 15
- FWCI
- 8.53
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Molecular Microbiology (publishedVersion)
- PubMed (publishedVersion)
- Figshare (submittedVersion, cc-by)
- Funders
- Biotechnology and Biological Sciences Research Council
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Keywords
- Vibrio cholerae, ferric uptake regulator, Fur protein, crystal structure, zinc binding site, iron homeostasis, metalloregulation, bacterial pathogenesis, therapeutic target
- MeSH terms
- Bacterial Proteins, Binding Sites, Cloning, Molecular, Metalloproteins, Metals, Repressor Proteins, Vibrio cholerae, Protein Structure, Tertiary
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