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Cited by 326Enzyme Structure and FunctionIron Metabolism and DisordersBacterial Genetics and Biotechnology

The DOI matches its Crossref record; 62 of the 62 references it cites were found in a registry or an index.

Architecture of a protein central to iron homeostasis: crystal structure and spectroscopic analysis of the ferric uptake regulator

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Pohl, Ehmke, Haller, Jon C., Mijovilovich, Ana, Meyer‐Klaucke, Wolfram, Garman, Elspeth, Vasil, Michael L.·2003·Molecular Microbiology
DOI 10.1046/j.1365-2958.2003.03337.x
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Abstract

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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Research works printed but not linked: 1

  1. Barton H.A.(1997)Structure and functional analysis of Pseudomonas aeruginosa Fur repressor.PhD Thesis University of Colorado Health Sciences Center.

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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
ORCID
Venue
Molecular Microbiology
Publisher
Wiley
Published
2003-02
Volume
47
Issue
4
Pages
903-915
ISSN
  • 0950-382X (ISSN-L)
  • 1365-2958
DOI
10.1046/j.1365-2958.2003.03337.x
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
Licence
onlinelibrary.wiley.com/termsAndConditions#vor (vor, 4 d)
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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