ArticleThe Journal of biological chemistry2009
Oligomeric structure of colicin ia channel in lipid bilayer membranes.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- Salt bridge disruption in colicin Ib channel-forming domain enhances membrane translocation and bactericidal activity.Journal of structural biology: X · 2026Article
- Pore-Forming Proteins: From Pore Assembly to Structure by Quantitative Single-Molecule Imaging.International journal of molecular sciences · 2023Review
- Bacterial pore-forming toxins.Microbiology (Reading, England) · 2022Article
- Pore formation by dimeric Bak and Bax: an unusual pore?Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Review
- Assembling the puzzle: Oligomerization of α-pore forming proteins in membranes.Biochimica et biophysica acta · 2016Review
- Pore-forming toxins: ancient, but never really out of fashion.Nature reviews. Microbiology · 2016Review
- APOL1 toxin, innate immunity, and kidney injury.Kidney international · 2015Review
- Article
- Review
- Obstructing toxin pathways by targeted pore blockage.Chemical reviews · 2012Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Colicin Ia is a soluble, harpoon-shaped bacteriocin which translocates across the periplasmic space of sensitive Escherichia coli cell by parasitizing an outer membrane receptor and forms voltage-gated ion channels in the inner membrane. This process leads to cell death, which has been thought to be caused by a single colicin Ia molecule. To directly visualize the three-dimensional structure of the channel, we generated two-dimensional crystals of colicin Ia inserted in lipid-bilayer membranes and determined a approximately 17 three-dimensional model by electron crystallography. Supported by velocity sedimentation, chemical cross-linking and single-particle image analysis, the three-dimensional structure is a crown-shaped oligomer enclosing a approximately 35 A-wide extrabilayer vestibule. Our study suggests that lipid insertion instigates a global conformational change in colicin Ia and that more than one molecule participates in the channel architecture with the vestibule, possibly facilitating the known large scale peptide translocation upon channel opening.
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Registered trials
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