ArticleCommunications biology2021
Cryo-EM reveals unique structural features of the FhuCDB Escherichia coli ferrichrome importer.
Article in Communications biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Cryo-electron microscopy structure of a zinc uptake ABC transporter.Structure (London, England : 1993) · 2026Article
- Article
- Modulating backbone flexibility in hydroxamate siderophores for improved iron chelation and peptide nucleic acid delivery into bacteria.The Biochemical journal · 2026Article
- Development of an inhibitory monoclonal nanobody targeting Streptococcus pyogenes siderophore binding protein FtsB.The Journal of biological chemistry · 2026Article
- Ferrichrome: bacterial function, synthetic mimics, and biomedical applications.Frontiers in microbiology · 2026Review
- Cryo-electron microscopy structure of a zinc uptake ABC transporter.bioRxiv : the preprint server for biology · 2025Article
- New insights into iron uptake in Streptococcus mutans: evidence for a role of siderophore-like molecules.Archives of microbiology · 2025Article
- Bioinformatics and modelling studies of FhuD, the periplasmic siderophore binding protein from the plant pathogen Erwinia amylovora.PloS one · 2025Article
- Rhizosphere domestication enhances root colonization and plant growth promotion performance ofFrontiers in microbiology · 2025Article
- Location, Location, Location: Establishing Design Principles for New Antibacterials from Ferric Siderophore Transport Systems.Molecules (Basel, Switzerland) · 2024Review
- Actinobacterial chalkophores: the biosynthesis of hazimycins.The Journal of antibiotics · 2024Article
Corrections and comments
- Erratum issued
Authors and funding
2 authors.
Funding
Abstract
As one of the most elegant biological processes developed in bacteria, the siderophore-mediated iron uptake demands the action of specific ATP-binding cassette (ABC) importers. Although extensive studies have been done on various ABC importers, the molecular basis of these iron-chelated-siderophore importers are still not fully understood. Here, we report the structure of a ferrichrome importer FhuCDB from Escherichia coli at 3.4 Å resolution determined by cryo electron microscopy. The structure revealed a monomeric membrane subunit of FhuB with a substrate translocation pathway in the middle. In the pathway, there were unique arrangements of residues, especially layers of methionines. Important residues found in the structure were interrogated by mutagenesis and functional studies. Surprisingly, the importer's ATPase activity was decreased upon FhuD binding, which deviated from the current understanding about bacterial ABC importers. In summary, to the best of our knowledge, these studies not only reveal a new structural twist in the type II ABC importer subfamily, but also provide biological insights in the transport of iron-chelated siderophores.
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