FhuA, a transporter of the Escherichia coli outer membrane, is converted into a channel upon binding of bacteriophage T5

• Published in: The EMBO journal Vol. 15; no. 8; pp. 1850 - 1856
• Main Authors: Bonhivers, M., Ghazi, A., Boulanger, P., Letellier, L.
• Format: Journal Article
• Language: English
• Published: England 15.04.1996
• Subjects: Bacterial Outer Membrane Proteins - chemistry; Bacterial Outer Membrane Proteins - isolation & purification; Bacterial Outer Membrane Proteins - metabolism; Bacteriophages - metabolism; Binding Sites; Escherichia coli; Escherichia coli - chemistry; Escherichia coli - metabolism; Escherichia coli - virology; Escherichia coli Proteins; Ferrichrome - metabolism; Ion Channel Gating; Ion Channels - chemistry; Ion Channels - metabolism; Lipid Bilayers; phage T5; Receptors, Virus - chemistry; Receptors, Virus - isolation & purification; Receptors, Virus - metabolism; Sodium Dodecyl Sulfate - pharmacology; T-Phages - metabolism

The Escherichia coli outer membrane protein FhuA catalyzes the transport of Fe3+(‐)ferrichrome and is the receptor of phage T5 and phi 80. The purified protein inserted into planar lipid bilayers showed no channel activity. Binding of phage T5 and FhuA resulted in the appearance of high conductance...