ArticleThe EMBO journal2007
Structure of colicin I receptor bound to the R-domain of colicin Ia: implications for protein import.
Article in The EMBO journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.
What it found
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Who cites it
62 citing papers in PubMed, 113 citations in OpenAlex.
- Design and Immunogenicity of a Nanoparticle Combination Vaccine for Salmonella in Poultry.Plant biotechnology journal · 2026Article
- The Correlation between Binding and Transport of a Siderophore Complex through Its TonB-Dependent Transporter.ACS omega · 2026Article
- Salt bridge disruption in colicin Ib channel-forming domain enhances membrane translocation and bactericidal activity.Journal of structural biology: X · 2026Article
- Bacteriocin biophysics: From protein-protein interaction models to navigators of the bacterial cell envelope.The Journal of biological chemistry · 2026Article
- Internal Ion Pairs Control Transport Through TonB-Dependent Siderophore Receptors.International journal of molecular sciences · 2026Article
- Proteolytically activated antibacterial toxins inhibit the growth of diverse gram-positive bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structural insights into Cir-mediated killing by the antimicrobial protein Microcin V.Communications biology · 2025Article
- Surface protein machineries in Gram-negative bacteria.Journal of cell science · 2025Review
- Isolation and characterization of novel bacteriophages targeting Stenotrophomonas maltophilia.Scientific reports · 2025Article
- Global quantitative proteome analysis of a multi-resistantFrontiers in microbiology · 2025Article
- Synthesis of colicin Ia neoglycoproteins: tools towards glyco-engineering of bacterial cell surfaces.RSC advances · 2024Article
- Location, Location, Location: Establishing Design Principles for New Antibacterials from Ferric Siderophore Transport Systems.Molecules (Basel, Switzerland) · 2024Review
- Chaperone-assisted cryo-EM structure ofbioRxiv : the preprint server for biology · 2024Article
- Chaperone-assisted cryo-EM structure of P. aeruginosa PhuR reveals molecular basis for heme binding.Structure (London, England : 1993) · 2024Article
- Genomic characterization of extended-spectrum beta-lactamase-producing and carbapenem-resistant Escherichia coli from urban wastewater in Australia.MicrobiologyOpen · 2024Article
- Specificity and mechanism of TonB-dependent ferric catecholate uptake by Fiu.Frontiers in microbiology · 2024Article
- Article
- Emergence of High-Level Cefiderocol Resistance in Carbapenem-Resistant Klebsiella pneumoniae from Bloodstream Infections in Patients with Hematologic Malignancies in China.Microbiology spectrum · 2022Article
- Growth-stage-related shifts in diatom endometabolome composition set the stage for bacterial heterotrophy.ISME communications · 2022Article
- Bacterial pore-forming toxins.Microbiology (Reading, England) · 2022Article
2 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
Colicin Ia is a 69 kDa protein that kills susceptible Escherichia coli cells by binding to a specific receptor in the outer membrane, colicin I receptor (70 kDa), and subsequently translocating its channel forming domain across the periplasmic space, where it inserts into the inner membrane and forms a voltage-dependent ion channel. We determined crystal structures of colicin I receptor alone and in complex with the receptor binding domain of colicin Ia. The receptor undergoes large and unusual conformational changes upon colicin binding, opening at the cell surface and positioning the receptor binding domain of colicin Ia directly above it. We modelled the interaction with full-length colicin Ia to show that the channel forming domain is initially positioned 150 A above the cell surface. Functional data using full-length colicin Ia show that colicin I receptor is necessary for cell surface binding, and suggest that the receptor participates in translocation of colicin Ia across the outer membrane.
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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.