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

@article{Pohl2003ArchitectureOA,
  title={Architecture of a protein central to iron homeostasis: crystal structure and spectroscopic analysis of the ferric uptake regulator},
  author={Ehmke Pohl and Jon C. Haller and Ana Mijovilovich and Wolfram Meyer‐Klaucke and Elspeth F. Garman and Michael L. Vasil},
  journal={Molecular Microbiology},
  year={2003},
  volume={47}
}
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… 
Crystal Structure and Function of the Zinc Uptake Regulator FurB from Mycobacterium tuberculosis*
TLDR
The crystal structure of FurB from Mycobacterium tuberculosis is reported and it is revealed that M. tuberculosis FurB is Zn(II)-dependent and is likely to control genes involved in the bacterial zinc uptake.
Iron Binding Site in a Global Regulator in Bacteria - Ferric Uptake Regulator (Fur) Protein: Structure, Mössbauer Properties, and Functional Implication.
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Results of the first quantum chemical investigation of various first- and second-shell models and experimental Mössbauer data of E. Coli Fur are presented, including the first robust evidence that site 2 is the Fe binding site with a 3His/2Glu ligand set, being the first case in non-heme proteins.
Ferric uptake regulator protein: Binding free energy calculations and per‐residue free energy decomposition
TLDR
Simulation results suggest that the formerly proposed site 2 is, in fact, the regulatory iron‐sensing site, and free energy decomposition analysis reveals a number of amino acids potentially important in dimerization and in DNA binding.
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TLDR
DNA protection and circular dichroism experiments demonstrate that, while these two sites influence the affinity of HpFur for DNA, only one is absolutely required for DNA binding and could be responsible for the conformational changes of Fur upon metal binding while the other is a secondary site.
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TLDR
A comprehensive overview of the crystal structure of Fur family metalloregulators is presented with a specific focus on the new structures of these TFs bound to DNA.
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TLDR
Another tetrameric structure of a PaFur mutant containing manganese and zinc metal ions is described and it is proposed that some conserved residues prevent the tetramerization in the subfamily of dimeric Fur.
Crystal structure of the Vibrio cholerae ferric uptake regulator (Fur) reveals insights into metal co‐ordination
TLDR
The crystal structure of V. cholerae Fur is presented that reveals a very different orientation of the DNA‐binding domains compared with that observed in Pseudomonas aeruginosa Fur, suggesting that in fact the Zn2 site is the regulatory iron binding site and theZn1 site plays an auxiliary role.
Functional specialization within the Fur family of metalloregulators
TLDR
There is a tremendous diversity in metal selectivity and biological function within the Fur family which includes sensors of iron (Fur), zinc (Zur), manganese (Mur), and nickel (Nur), and the mechanism of metal ion sensing by Fur family proteins is still controversial.
Quaternary Structure of Fur Proteins, a New Subfamily of Tetrameric Proteins.
TLDR
This study purified Fur from four pathogenic strains and compared them to Fur from Escherichia coli, and showed that the dissociation of the tetramers into dimers is necessary for binding of Fur to DNA, and that this dissociation requires the combined effect of metal ion binding and DNA proximity.
The conformational stability and thermodynamics of Fur A (ferric uptake regulator) from Anabaena sp. PCC 7119.
TLDR
The stability, thermodynamics and structure of the functional dimeric Fur A from Anabaena sp.
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