Disease relevance of fur

• Escherichia coli Fur is usually isolated as a homodimer with two metal sites per subunit [1].
• Functional characterization of the dimerization domain of the ferric uptake regulator (Fur) of Pseudomonas aeruginosa [2].

High impact information on fur

• Reduction of the disulfide bridges causes only local structure variations, whereas zinc addition to reduced Fur induces protein dimerization [1].
• Ferric uptake regulator (Fur) is a global bacterial regulator that uses iron as a cofactor to bind to specific DNA sequences [1].
• Transcription of perR was autoregulated, and PerR repressed transcription of the iron homeostasis regulator Fur, which is a positive regulator of catalase expression [3].
• Thus, these regulators may sense the physiological consequences of extraneous Fe concentrations, rather than the concentration of Fe per se, as happens in those bacteria (e.g. Escherichia coli) in which the ferric uptake regulator Fur is the global Fe-responsive gene regulator [4].

Analytical, diagnostic and therapeutic context of fur

• Structural changes of Escherichia coli ferric uptake regulator during metal-dependent dimerization and activation explored by NMR and X-ray crystallography [1].

References