ArticleStructure (London, England : 1993)2008
Colicin N binds to the periphery of its receptor and translocator, outer membrane protein F.
Article in Structure (London, England : 1993), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 48 citations in OpenAlex.
- Interaction of Tryptophan- and Arginine-Rich Antimicrobial Peptide withInternational journal of molecular sciences · 2023Article
- Genomic discovery and structural dissection of a novel type of polymorphic toxin system in gram-positive bacteria.Computational and structural biotechnology journal · 2022Article
- Diversity of Contact-Dependent Growth Inhibition Systems ofJournal of bacteriology · 2019Review
- Emerging Diversity in Lipid-Protein Interactions.Chemical reviews · 2019Review
- Similarities and Differences between Colicin and Filamentous Phage Uptake by Bacterial Cells.EcoSal Plus · 2019Review
- Determining the amphipol distribution within membrane-protein fibre samples using small-angle neutron scattering.Acta crystallographica. Section D, Structural biology · 2018Article
- Gram-negative trimeric porins have specific LPS binding sites that are essential for porin biogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Genome-Wide Screening Identifies Six Genes That Are Associated with Susceptibility to Escherichia coli Microcin PDI.Applied and environmental microbiology · 2015Article
- Outer membrane protein F stabilised with minimal amphipol forms linear arrays and LPS-dependent 2D crystals.The Journal of membrane biology · 2014Article
- The antibacterial toxin colicin N binds to the inner core of lipopolysaccharide and close to its translocator protein.Molecular microbiology · 2014Article
- Daring to be different: colicin N finds another way.Molecular microbiology · 2014Article
- Low resolution structure and dynamics of a colicin-receptor complex determined by neutron scattering.The Journal of biological chemistry · 2012Article
- Interaction of nuclease colicins with membranes: insertion depth correlates with bilayer perturbation.PloS one · 2012Article
- Directed epitope delivery across the Escherichia coli outer membrane through the porin OmpF.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Swimming against the tide: progress and challenges in our understanding of colicin translocation.Nature reviews. Microbiology · 2010Review
- The colicin Ia receptor, Cir, is also the translocator for colicin Ia.Molecular microbiology · 2010Article
- The crystal structure of the TolB box of colicin A in complex with TolB reveals important differences in the recruitment of the common TolB translocation portal used by group A colicins.Molecular microbiology · 2010Article
- Allosteric beta-propeller signalling in TolB and its manipulation by translocating colicins.The EMBO journal · 2009Article
- Genome-wide screens: novel mechanisms in colicin import and cytotoxicity.Molecular microbiology · 2009Article
- Energy-dependent immunity protein release during tol-dependent nuclease colicin translocation.The Journal of biological chemistry · 2009Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Colicins kill Escherichia coli after translocation across the outer membrane. Colicin N displays an unusually simple translocation pathway, using the outer membrane protein F (OmpF) as both receptor and translocator. Studies of this binary complex may therefore reveal a significant component of the translocation pathway. Here we show that, in 2D crystals, colicin is found outside the porin trimer, suggesting that translocation may occur at the protein-lipid interface. The major lipid of the outer leaflet interface is lipopolysaccharide (LPS). It is further shown that colicin N binding displaces OmpF-bound LPS. The N-terminal helix of the pore-forming domain, which is not required for pore formation, rearranges and binds to OmpF. Colicin N also binds artificial OmpF dimers, indicating that trimeric symmetry plays no part in the interaction. The data indicate that colicin is closely associated with the OmpF-lipid interface, providing evidence that this peripheral pathway may play a role in colicin transmembrane transport.
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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.