ArticleJournal of bacteriology2002
Surface loop motion in FepA.
Article in Journal of bacteriology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
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Who cites it
15 citing papers in PubMed, 34 citations in OpenAlex.
- Specificity and mechanism of TonB-dependent ferric catecholate uptake by Fiu.Frontiers in microbiology · 2024Article
- Iron Acquisition Systems of Gram-negative Bacterial Pathogens Define TonB-Dependent Pathways to Novel Antibiotics.Chemical reviews · 2021Review
- The complex of ferric-enterobactin with its transporter from Pseudomonas aeruginosa suggests a two-site model.Nature communications · 2019Article
- ROSET Model of TonB Action in Gram-Negative Bacterial Iron Acquisition.Journal of bacteriology · 2016Review
- Concerted loop motion triggers induced fit of FepA to ferric enterobactin.The Journal of general physiology · 2014Article
- Importance of porins for biocide efficacy against Mycobacterium smegmatis.Applied and environmental microbiology · 2011Article
- Kinetic analysis of ligand interaction with the gonococcal transferrin-iron acquisition system.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2009Article
- Fluoresceination of FepA during colicin B killing: effects of temperature, toxin and TonB.Molecular microbiology · 2009Article
- TonB induces conformational changes in surface-exposed loops of FhuA, outer membrane receptor of Escherichia coli.Protein science : a publication of the Protein Society · 2008Article
- Insight from TonB hybrid proteins into the mechanism of iron transport through the outer membrane.Journal of bacteriology · 2008Article
- FepA- and TonB-dependent bacteriophage H8: receptor binding and genomic sequence.Journal of bacteriology · 2007Article
- Evidence of ball-and-chain transport of ferric enterobactin through FepA.The Journal of biological chemistry · 2007Article
- Defined inactive FecA derivatives mutated in functional domains of the outer membrane transport and signaling protein of Escherichia coli K-12.Journal of bacteriology · 2004Article
- Recognition of ferric catecholates by FepA.Journal of bacteriology · 2004Article
- Molecular basis of bacterial outer membrane permeability revisited.Microbiology and molecular biology reviews : MMBR · 2003Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Using a lysine-specific cleavable cross-linking reagent ethylene glycolbis(sulfosuccimidylsuccinate) (Sulfo-EGS), we studied conformational motion in the surface loops of Escherichia coli FepA during its transport of the siderophore ferric enterobactin. Site-directed mutagenesis determined that Sulfo-EGS reacted with two lysines, K332 and K483, and at least two other unidentified Lys residues in the surface loops of the outer membrane protein. The reagent cross-linked K483 in FepA L7 to either K332 in L5, forming a product that we designated band 1, or to the major outer membrane proteins OmpF, OmpC, and OmpA, forming band 2. Ferric enterobactin binding to FepA did not prevent modification of K483 by Sulfo-EGS but blocked its cross-linking to OmpF/C and OmpA and reduced its coupling to K332. These data show that the loops of FepA undergo conformational changes in vivo, with an approximate magnitude of 15 A, from a ligand-free open state to a ligand-bound closed state. The coupling of FepA L7 to OmpF, OmpC, or OmpA was TonB independent and was unaffected by the uncouplers CCCP (carbonyl cyanide m-chlorophenylhydrazone) and DNP (2,4-dinitrophenol) but completely inhibited by cyanide.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.