ArticleJournal of bacteriology2007
Docking of the periplasmic FecB binding protein to the FecCD transmembrane proteins in the ferric citrate transport system of Escherichia coli.
Article in Journal of bacteriology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 50 citations in OpenAlex.
- Revealing the nuclearity of iron citrate complexes at biologically relevant conditions.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2024Article
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- Identification of the iron-limitation stimulon in Staphylococcus lugdunensis.Archives of microbiology · 2021Article
- The ATP-Binding Cassette (ABC) Transport Systems inBiology · 2020Review
- Transcriptome profile of Corynebacterium pseudotuberculosis in response to iron limitation.BMC genomics · 2019Article
- Chemical Genetic Interaction Profiling Reveals Determinants of Intrinsic Antibiotic Resistance in Mycobacterium tuberculosis.Antimicrobial agents and chemotherapy · 2017Article
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- Does a voltage-sensitive outer envelope transport mechanism contributes to the chloroplast iron uptake?Planta · 2016Article
- Pyrophosphate-mediated iron acquisition from transferrin in Neisseria meningitidis does not require TonB activity.PloS one · 2014Article
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- Adaptative biochemical pathways and regulatory networks in Klebsiella oxytoca BAS-10 producing a biotechnologically relevant exopolysaccharide during Fe(III)-citrate fermentation.Microbial cell factories · 2012Article
- Bacillus cereus iron uptake protein fishes out an unstable ferric citrate trimer.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Genome-wide transcriptional response of the archaeon Thermococcus gammatolerans to cadmium.PloS one · 2012Article
- Specificity of Staphyloferrin B recognition by the SirA receptor from Staphylococcus aureus.The Journal of biological chemistry · 2010Article
- The Staphylococcus aureus siderophore receptor HtsA undergoes localized conformational changes to enclose staphyloferrin A in an arginine-rich binding pocket.The Journal of biological chemistry · 2010Article
- The second extracellular loop of pore-forming subunits of ATP-binding cassette transporters for basic amino acids plays a crucial role in interaction with the cognate solute binding protein(s).Journal of bacteriology · 2010Article
- The ferrichrome uptake pathway in Pseudomonas aeruginosa involves an iron release mechanism with acylation of the siderophore and recycling of the modified desferrichrome.Journal of bacteriology · 2010Article
- The ATP-binding cassette transporter Cbc (choline/betaine/carnitine) recruits multiple substrate-binding proteins with strong specificity for distinct quaternary ammonium compounds.Molecular microbiology · 2010Article
- Lactobacillus plantarum WCFS1 electron transport chains.Applied and environmental microbiology · 2009Article
- Toxin-antitoxin systems in Escherichia coli influence biofilm formation through YjgK (TabA) and fimbriae.Journal of bacteriology · 2009Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Citrate-mediated iron transport across the cytoplasmic membrane is catalyzed by an ABC transporter that consists of the periplasmic binding protein FecB, the transmembrane proteins FecC and FecD, and the ATPase FecE. Salt bridges between glutamate residues of the binding protein and arginine residues of the transmembrane proteins are predicted to mediate the positioning of the substrate-loaded binding protein on the transmembrane protein, based on the crystal structures of the ABC transporter for vitamin B(12), consisting of the BtuF binding protein and the BtuCD transmembrane proteins (E. L. Borths et al., Proc. Natl. Acad. Sci. USA 99:16642-16647, 2002). Here, we examined the role of the residues predicted to be involved in salt-bridge formation between FecB and FecCD by substituting these residues with alanine, cysteine, arginine, and glutamate and by analyzing the citrate-mediated iron transport of the mutants. Replacement of E93 in FecB with alanine [FecB(E93A)], cysteine, or arginine nearly abolished citrate-mediated iron transport. Mutation FecB(E222R) nearly eliminated transport, and FecB(E222A) and FecB(E222C) strongly reduced transport. FecD(R54C) and FecD(R51E) abolished transport, whereas other R-to-C mutations in putative interaction sites between FecCD and FecB substantially reduced transport. The introduced cysteine residues in FecB and FecCD also served to examine the formation of disulfide bridges in place of salt bridges between the binding protein and the transmembrane proteins. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis results suggest cross-linking of FecB(E93C) to FecD(R54C) and FecB(E222C) to FecC(R60C). The data are consistent with the proposal that FecB(E93) is contained in the region that binds to FecD and FecB(E222) in the region that binds to FecC.
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