The DOI matches its Crossref record; 51 of the 51 references it cites were found in a registry or an index.
Crystal structure of the Vibrio cholerae ferric uptake regulator (Fur) reveals insights into metal co‐ordination
Open accessAbstract
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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The cited source doesn’t support the claim as written.
In the citing paper
“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]
Checked by a reasoning model — may be wrong.
Experimental — accuracy not yet measuredIn the citing paper
“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]
In the citing paper
“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]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
[20] Processing of X-ray diffraction data collected in oscillation mode
Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475
Coot : model-building tools for molecular graphics
Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571
Clustal W and Clustal X version 2.0
Larkin, M., Blackshields, G., Brown, N. P., Chenna, R., McGettigan, P., McWilliam, H., Valentin, F., Wallace, I. M., Wilm, A., López, R., et al. (2007) · Bioinformatics · doi:10.1093/bioinformatics/btm404 · Cited by 28,598
Phaser crystallographic software
McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C., & Read, R. J. (2007) · Journal of Applied Crystallography · doi:10.1107/s0021889807021206 · Cited by 20,612
The PyMOL Molecular Graphics System
DeLano, W. L. (2002) · Medical Entomology and Zoology · Cited by 18,147
The CCP4 suite: programs for protein crystallography
Number Collaborative Computational Project (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994003112 · Cited by 17,317
Refinement of Macromolecular Structures by the Maximum-Likelihood Method
Murshudov, G. N., Vagin, A. A., & Dodson, E. J. (1997) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444996012255 · Cited by 14,796
Electrostatics of nanosystems: Application to microtubules and the ribosome
Baker, N., Sept, D., Joseph, S., Holst, M., & McCammon, J. A. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.181342398 · Cited by 7,125
PHENIX : building new software for automated crystallographic structure determination
Adams, P. D., Grosse-Kunstleve, R. W., Hung, L.-W., Ioerger, T. R., McCoy, A. J., Moriarty, N. W., Read, R. J., Sacchettini, J. C., Sauter, N. K., & Terwilliger, T. C. (2002) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444902016657 · Cited by 4,361
Andrews, S. C., Robinson, A. K., & Rodríguez-Quiñones, F. (2003) · FEMS Microbiology Reviews · doi:10.1016/s0168-6445(03)00055-x · Cited by 2,702
Cited by
Sorted by citations
Items 101–125 of 125
Purification and characterization of Campylobacter jejuni ferric uptake regulator
Sarvan, S., Yeung, A., Charih, F., Stintzi, A. P., & Couture, J. (2019) · BioMetals · doi:10.1007/s10534-019-00177-5 · Cited by 6
Chakraborty, R. (2013) · Springer briefs in molecular science · doi:10.1007/978-94-007-6088-2_1 · Cited by 6
Chen, J., Wang, M., Liu, H., & Li, Z. (2025) · Environmental Science & Technology · doi:10.1021/acs.est.5c10489 · Cited by 5
Barker, R. A., Tisnado, J., Lambert, L. A., Gärdes, A., Carrano, M. W., Carrano, P. N., Gillian, C., & Carrano, C. J. (2014) · BioMetals · doi:10.1007/s10534-014-9815-7 · Cited by 5
Yu, C., A, C. A. L., Hu, H., Xia, Y., Freedman, D. S., Reddington, A. P., Daaboul, G. G., Ünlü, M. S., & Genco, C. A. (2014) · PLoS ONE · doi:10.1371/journal.pone.0096832 · Cited by 5
Metals in Cells: Control of Cellular Metal Concentration
Gilston, B. A., & O’Halloran, T. V. (2004) · Wiley eBooks · doi:10.1002/9781119951438.eibc2107 · Cited by 6
Zane, H. K., & Butler, A. (2013) · Elsevier eBooks · doi:10.1016/b978-0-08-097774-4.00301-6 · Cited by 4
Najafi, F., Purcell, A. G., Homes, F. H., & Ding, H. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110702 · Cited by 3
“…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 the DNA-binding domain and the dimerization domain; and site 3 (coordinated by Cys-93 and Cys-96) is at the C-terminal end of the dimerization domain (10, 12).”
InfluentialFontenot, C. R., Hoepner, T., Xiong, J., Ding, H., & Popescu, C. V. (2025) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2025.112928 · Cited by 3
Argandoña, Y., Olivos, A., Obando, P., Imas, F., Pohl, E., Quatrini, R., & Arenas-Salinas, M. (2025) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2025.02.017 · Cited by 3
Parent, A., Caux‐Thang, C., Signor, L., Clémancey, M., Ramakrishnan, S., Blondin, G., Maldivi, P., Duarte, V., & Latour, J. (2013) · Angewandte Chemie · doi:10.1002/ange.201304021 · Cited by 3
Sensing Metals: the Versatility of Fur
Cha, S., Shin, J., & Roe, J. (2014) · ASM Press eBooks · doi:10.1128/9781555816841.ch12 · Cited by 2
Liu, Z., Chen, Z., & Wu, W. (2012) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s1744309112024311 · Cited by 1
Comparative genomics reveals ‘novel’ Fur regulated sRNAs and coding genes in diverse proteobacteria
Sridhar, J., Sabarinathan, R., Gunasekaran, P., & Sekar, K. (2012) · Gene · doi:10.1016/j.gene.2012.12.057 · Cited by 1
Response of Foodborne Pathogens to Oxidative Stress
Rakhi, N. N., Bari, L., & Rahaman, M. M. (2022) · Springer eBooks · doi:10.1007/978-3-030-90578-1_6 · Cited by 1
Khalil, S. (2011) · Spectrum Research Repository (Concordia University) · Cited by 1
Crichton, R. R. (2016) · Wiley eBooks · doi:10.1002/9781118925645.ch3 · Cited by 1
Iron Regulation and Virulence in Gram-Negative Bacterial Pathogens withYersinia pestisas a Paradigm
Perry, R. D., & McDonough, K. A. (2016) · ASM Press eBooks · doi:10.1128/9781555818524.ch6
Experimental phasing using zinc and sulfur anomalous signals measured at the zinc absorption peak
Lee, S.-M., Kim, M., Ji, C., Lee, J., & Cha, S. (2013) · The Journal of Microbiology · doi:10.1007/s12275-013-3412-2
Hamed, M. Y., & Jabour, S. (2020) · Preprints.org · doi:10.20944/preprints202011.0146.v2
Hamed, M. Y., & Jabour, S. (2020) · Preprints.org · doi:10.20944/preprints202011.0146.v3
Hamed, M. Y., & Jabour, S. (2020) · Preprints.org · doi:10.20944/preprints202011.0146.v4
Métabolisme du fer et de l'hème chez Lactobacillus sakei
Duhutrel, P. (2011) · theses.fr (ABES) · doi:10.70675/bfd9ff84z3925z4f76z96deza9085c27340b
Salyamov, V., Kostareva, O. S., Mayorov, S. G., Tishchenko, S. V., Gabdulkhakov, A. G., Nagel, A. S., Andreeva‐Kovalevskaya, Z. I., Siunov, A. V., & Solonin, A. S. (2026) · Molecular Biology · doi:10.1134/s0026893326700251
Metadata
- 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
- 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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
