ArticleProtein science : a publication of the Protein Society2000
Crystal structure of the antibiotic albomycin in complex with the outer membrane transporter FhuA.
Article in Protein science : a publication of the Protein Society, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
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55 citing papers in PubMed, 162 citations in OpenAlex.
- Covalent Chemical Tagging of Transmembrane Transport Proteins Illuminates the Internalization Pathways of Xenosiderophores.Journal of the American Chemical Society · 2026Article
- Perspective Approaches to "Trojan Horse" Strategy Development for Combating Bacterial Pathogens.Pharmaceuticals (Basel, Switzerland) · 2026Review
- Characterization of C3' Epimerization of the Thioheptose Core in the Biosynthesis of AlbomycinACS catalysis · 2025Article
- Fimsbactin Siderophores From a South African Marine Sponge Symbiont, Marinomonas sp. PE14-40.Microbial biotechnology · 2025Article
- Exploring heme and iron acquisition strategies of Porphyromonas gingivalis-current facts and hypotheses.FEMS microbiology reviews · 2025Review
- Substrate Uptake by TonB-Dependent Outer Membrane Transporters.Molecular microbiology · 2024Review
- Location, Location, Location: Establishing Design Principles for New Antibacterials from Ferric Siderophore Transport Systems.Molecules (Basel, Switzerland) · 2024Review
- Whole-Cell Biosensor for Iron Monitoring as a Potential Tool for Safeguarding Biodiversity in Polar Marine Environments.Marine drugs · 2024Review
- Siderophores as tools and treatments.npj antimicrobials and resistance · 2024Review
- Characterization of the Attachment of Three New Coliphages onto the Ferrichrome Transporter FhuA.Journal of virology · 2023Article
- Energization of Outer Membrane Transport by the ExbB ExbD Molecular Motor.Journal of bacteriology · 2023Review
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- Structural basis for host recognition and superinfection exclusion by bacteriophage T5.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- The chemistry and biology of natural ribomimetics and related compounds.RSC chemical biology · 2022Review
- Biosynthesis and Chemical Synthesis of Albomycin Nucleoside Antibiotics.Antibiotics (Basel, Switzerland) · 2022Review
- Natural Trojan horse inhibitors of aminoacyl-tRNA synthetases.RSC chemical biology · 2021Review
- TonB-Dependent Transporters in Sphingomonads: Unraveling Their Distribution and Function in Environmental Adaptation.Microorganisms · 2020Review
- Identification of the Enzymes Mediating the Maturation of the Seryl-tRNA Synthetase Inhibitor SB-217452 during the Biosynthesis of Albomycins.Angewandte Chemie (International ed. in English) · 2020Article
- Antibody-recruiting protein-catalyzed capture agents to combat antibiotic-resistant bacteria.Chemical science · 2020Article
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
One alternative method for drug delivery involves the use of siderophore-antibiotic conjugates. These compounds represent a specific means by which potent antimicrobial agents, covalently linked to iron-chelating siderophores, can be actively transported across the outer membrane of gram-negative bacteria. These "Trojan Horse" antibiotics may prove useful as an efficient means to combat multi-drug-resistant bacterial infections. Here we present the crystallographic structures of the natural siderophore-antibiotic conjugate albomycin and the siderophore phenylferricrocin, in complex with the active outer membrane transporter FhuA from Escherichia coli. To our knowledge, this represents the first structure of an antibiotic bound to its cognate transporter. Albomycins are broad-host range antibiotics that consist of a hydroxamate-type iron-chelating siderophore, and an antibiotically active, thioribosyl pyrimidine moiety. As observed with other hydroxamate-type siderophores, the three-dimensional structure of albomycin reveals an identical coordination geometry surrounding the ferric iron atom. Unexpectedly, this antibiotic assumes two conformational isomers in the binding site of FhuA, an extended and a compact form. The structural information derived from this study provides novel insights into the diverse array of antibiotic moieties that can be linked to the distal portion of iron-chelating siderophores and offers a structural platform for the rational design of hydroxamate-type siderophore-antibiotic conjugates.
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