PMID:11587645

Citation	Ferguson, AD, Ködding, J, Walker, G, Bös, C, Coulton, JW, Diederichs, K, Braun, V and Welte, W (2001) Active transport of an antibiotic rifamycin derivative by the outer-membrane protein FhuA. Structure 9:707-16
Abstract	FhuA, an integral membrane protein of Escherichia coli, actively transports ferrichrome and the structurally related antibiotic albomycin across the outer membrane. The transport is coupled to the proton motive force, which energizes FhuA through the inner-membrane protein TonB. FhuA also transports the semisynthetic rifamycin derivative CGP 4832, although the chemical structure of this antibiotic differs markedly from that of ferric hydroxamates.
Links	PubMed
Keywords	Allosteric Site; Bacterial Outer Membrane Proteins/chemistry; Bacterial Proteins/chemistry; Binding Sites; Biological Transport; Biological Transport, Active; Cell Membrane/metabolism; Crystallography, X-Ray; Dose-Response Relationship, Drug; Escherichia coli/chemistry; Escherichia coli Proteins/chemistry; Ferrichrome/chemistry; Ligands; Membrane Proteins/chemistry; Models, Molecular; Mutation; Protein Binding; Protein Structure, Tertiary; Receptors, Virus/chemistry; Rifamycins/chemistry; Rifamycins/pharmacology; Spectrometry, Fluorescence; Time Factors; Tryptophan/chemistry
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