Structural Changes of Escherichia coli Ferric Uptake Regulator during Metal-dependent Dimerization and Activation Explored by NMR and X-ray Crystallography

• Published in: The Journal of biological chemistry Vol. 281; no. 30; pp. 21286 - 21295
• Main Authors: Pecqueur, Ludovic, D'Autréaux, Benoît, Dupuy, Jérome, Nicolet, Yvain, Jacquamet, Lilian, Brutscher, Bernhard, Michaud-Soret, Isabelle, Bersch, Beate
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 28.07.2006; American Society for Biochemistry and Molecular Biology
• Subjects: Amino Acid Sequence; Bacterial Proteins - chemistry; Biochemistry; Biochemistry, Molecular Biology; Crystallography, X-Ray - methods; Dimerization; DNA - chemistry; Escherichia coli; Escherichia coli - metabolism; Life Sciences; Magnetic Resonance Spectroscopy - methods; Models, Molecular; Molecular Sequence Data; Protein Denaturation; Protein Folding; Protein Structure, Quaternary; Protein Structure, Secondary; Repressor Proteins - chemistry; Sequence Homology, Amino Acid; Zinc - chemistry

Ferric uptake regulator (Fur) is a global bacterial regulator that uses iron as a cofactor to bind to specific DNA sequences. Escherichia coli Fur is usually isolated as a homodimer with two metal sites per subunit. Metal binding to the iron site induces protein activation; however the exact role of...