ArticleJournal of bacteriology1995
Ferrichrome transport in Escherichia coli K-12: altered substrate specificity of mutated periplasmic FhuD and interaction of FhuD with the integral membrane protein FhuB.
Article in Journal of bacteriology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed.
- When less is more: Counterintuitive stoichiometries and cellular abundances are essential for ABC transporters' function.Science advances · 2025Article
- PQS and pyochelin inMicrobiology spectrum · 2024Article
- Enhancement of growth media for extreme iron limitation in Escherichia coli.Access microbiology · 2024Article
- Article
- Sequence, structure, and function of the Dps DNA-binding protein from Deinococcus wulumuqiensis R12.Microbial cell factories · 2022Article
- Biosynthesis and Chemical Synthesis of Albomycin Nucleoside Antibiotics.Antibiotics (Basel, Switzerland) · 2022Review
- Cryo-EM reveals unique structural features of the FhuCDB Escherichia coli ferrichrome importer.Communications biology · 2021Article
- Structural insights into a novel family of integral membrane siderophore reductases.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Iron Acquisition Systems of Gram-negative Bacterial Pathogens Define TonB-Dependent Pathways to Novel Antibiotics.Chemical reviews · 2021Review
- Ferric iron reductases and their contribution to unicellular ferrous iron uptake.Journal of inorganic biochemistry · 2021Review
- The Role of Ovotransferrin in Egg-White Antimicrobial Activity: A Review.Foods (Basel, Switzerland) · 2021Review
- Natural Trojan horse inhibitors of aminoacyl-tRNA synthetases.RSC chemical biology · 2021Review
- Substrate recognition and ATPase activity of theThe Journal of biological chemistry · 2020Article
- ATP binding and hydrolysis disrupt the high-affinity interaction between the heme ABC transporter HmuUV and its cognate substrate-binding protein.The Journal of biological chemistry · 2017Article
- An update on the transport and metabolism of iron in Listeria monocytogenes: the role of proteins involved in pathogenicity.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2015Review
- Mycobacteria, metals, and the macrophage.Immunological reviews · 2015Review
- The solution structure, binding properties, and dynamics of the bacterial siderophore-binding protein FepB.The Journal of biological chemistry · 2014Article
- Bordetella pertussis FbpA binds both unchelated iron and iron siderophore complexes.Biochemistry · 2014Article
- Two molybdate/tungstate ABC transporters that interact very differently with their substrate binding proteins.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Article
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3 authors.
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Abstract
FhuD is the periplasmic binding protein of the ferric hydroxamate transport system of Escherichia coli. FhuD was isolated and purified as a His-tag-labeled derivative on a Ni-chelate resin. The dissociation constants for ferric hydroxamates were estimated from the concentration-dependent decrease in the intrinsic fluorescence intensity of His-tag-FhuD and were found to be 0.4 microM for ferric aerobactin, 1.0 microM for ferrichrome, 0.3 microM for ferric coprogen, and 5.4 microM for the antibiotic albomycin. Ferrichrome A, ferrioxamine B, and ferrioxamine E, which are poorly taken up via the Fhu system, displayed dissociation constants of 79, 36, and 42 microM, respectively. These are the first estimated dissociation constants reported for a binding protein of a microbial iron transport system. Mutants impaired in the interaction of ferric hydroxamates with FhuD were isolated. One mutated FhuD, with a W-to-L mutation at position 68 [FhuD(W68L)], differed from wild-type FhuD in transport activity in that ferric coprogen supported promotion of growth of the mutant on iron-limited medium, while ferrichrome was nearly inactive. The dissociation constants of ferric hydroxamates were higher for FhuD(W68L) than for wild-type FhuD and lower for ferric coprogen (2.2 microM) than for ferrichrome (156 microM). Another mutated FhuD, FhuD(A150S, P175L), showed a weak response to ferrichrome and albomycin and exhibited dissociation constants two- to threefold higher than that of wild-type FhuD. Interaction of FhuD with the cytoplasmic membrane transport protein FhuB was studied by determining protection of FhuB degradation by trypsin and proteinase K and by cross-linking experiments. His-tag-FhuD and His-tag-FhuD loaded with aerobactin specifically prevented degradation of FhuB and were cross-linked to FhuB. FhuD loaded with substrate and also FhuD free of substrate were able to interact with FhuB.
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