Cited by 126Bacterial Genetics and BiotechnologyEnzyme Structure and FunctionIron Metabolism and Disorders

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Crystal structure of the Vibrio cholerae ferric uptake regulator (Fur) reveals insights into metal co‐ordination

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Sheikh, Md. Arif, Taylor, Garry L.·2009·Molecular Microbiology

DOI 10.1111/j.1365-2958.2009.06718.x

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Abstract

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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“Fur proteins exist as a dimer or tetramer (19), and each Fur monomer has three putative metal binding sites (13, 15): site 1 is located within the dimerization domain; site 2 connects the DNA binding domain and the dimerization domain, and site 3 is positioned at the C-terminal end of the…”
Background

Authors: Sheikh, M. A., & Taylor, G. L.
Affiliations: University of St Andrews (GB)
Corresponding author: Taylor, Garry L.
ORCID: Sheikh, Md. Arif
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
DOI: 10.1111/j.1365-2958.2009.06718.x
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
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor)
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
Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › 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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Crystal structure of the Vibrio cholerae ferric uptake regulator (Fur) reveals insights into metal co‐ordination

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