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Diffusion through channel derivatives of the Escherichia coli FhuA transport protein by Michael Braun; Helmut Killmann; Elke Maier; Roland Benz; Volkmar Braun is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Diffusion through channel derivatives of the Escherichia coli FhuA transport protein about?

FhuA is a multifunctional protein in the outer membrane of __Escherichia coli__ that actively transports [Fe^3+^]ferrichrome, the antibiotics albomycin and rifamycin CGP 4832, and mediates sensitivity of cells to the unrelated phages T5, T1, φ80 and UC‐1, and to colicin M and microcin J25. The energy source of active transport is the proton motive force of the cytoplasmic membrane that is required for all FhuA functions except for infection by phage T5. The FhuA crystal structure reveals 22 antiparallel transmembrane β‐strands that form a β‐barrel which is closed by a globular N‐terminal domain. FhuA still displays active transport and sensitivity to all ligands except microcin J25 when the globular domain (residues 5–160) is excised and supports weakly unspecific diffusion of substrates across the outer membrane. Here it is shown that isolated FhuAΔ5–160 supported diffusion of ions through artificial planar lipid bilayer membranes but did not form stable channels. The double mutant FhuAΔ5–160 Δ322–336 lacking in addition to the globular domain most of the large surface loop 4 which partially constricts the channel entrance, displayed an increased single‐channel conductance but for

Who reads Diffusion through channel derivatives of the Escherichia coli FhuA transport protein?

Author

Michael Braun; Helmut Killmann; Elke Maier; Roland Benz; Volkmar Braun

Publisher

John Wiley and Sons; Springer; Wiley (Blackwell Publishing); Springer-Verlag; Blackwell Publishing Inc.; Springer Verlag; Wiley; Springer Science and Business Media LLC (ISSN 1432-1327)

Published

2002

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)