ArticleThe Journal of biological chemistry2009
Structure and function of colicin S4, a colicin with a duplicated receptor-binding domain.
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 19 papers.
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Who cites it
19 citing papers in PubMed, 38 citations in OpenAlex.
- Salt bridge disruption in colicin Ib channel-forming domain enhances membrane translocation and bactericidal activity.Journal of structural biology: X · 2026Article
- Microcin C7 as a Potential Antibacterial-Immunomodulatory Agent in the Postantibiotic Era: Overview of Its Bioactivity Aspects and Applications.International journal of molecular sciences · 2024Review
- Story of Pore-Forming Proteins from Deadly Disease-Causing Agents to Modern Applications with Evolutionary Significance.Molecular biotechnology · 2024Review
- Bacterial pore-forming toxins.Microbiology (Reading, England) · 2022Article
- Diversity and prevalence of type VI secretion system effectors in clinicalFrontiers in microbiology · 2022Article
- β-Strand-mediated interactions of protein domains.Proteins · 2020Article
- Bacteriocin production by mucosal bacteria in current and previous colorectal neoplasia.BMC cancer · 2020Article
- Proteomic Analyses Reveal New Insights on the Antimicrobial Mechanisms of Chitosan Biopolymers and Their Nanosized Particles againstInternational journal of molecular sciences · 2019Article
- Colicin Z, a structurally and functionally novel colicin type that selectively kills enteroinvasive Escherichia coli and Shigella strains.Scientific reports · 2019Article
- Tools and Approaches for Dissecting Protein Bacteriocin Import in Gram-Negative Bacteria.Frontiers in microbiology · 2019Review
- Development of a biosensor protein bullet as a fluorescent method for fast detection of Escherichia coli in drinking water.PloS one · 2018Article
- Transcriptional Regulation of the Outer Membrane Porin Gene ompW Reveals its Physiological Role during the Transition from the Aerobic to the Anaerobic Lifestyle of Escherichia coli.Frontiers in microbiology · 2016Article
- The antibacterial toxin colicin N binds to the inner core of lipopolysaccharide and close to its translocator protein.Molecular microbiology · 2014Article
- The unstructured domain of colicin N kills Escherichia coli.Molecular microbiology · 2013Article
- The crystal structure of the lipid II-degrading bacteriocin syringacin M suggests unexpected evolutionary relationships between colicin M-like bacteriocins.The Journal of biological chemistry · 2012Article
- Structural and mechanistic studies of pesticin, a bacterial homolog of phage lysozymes.The Journal of biological chemistry · 2012Article
- Swimming against the tide: progress and challenges in our understanding of colicin translocation.Nature reviews. Microbiology · 2010Review
- Article
- Genome-wide screens: novel mechanisms in colicin import and cytotoxicity.Molecular microbiology · 2009Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Colicins are plasmid-encoded toxic proteins produced by Escherichia coli strains to kill other E. coli strains that lack the corresponding immunity protein. Colicins intrude into the host cell by exploiting existing transport, diffusion, or efflux systems. We have traced the way colicin S4 takes to execute its function and show that it interacts specifically with OmpW, OmpF, and the Tol system before it inserts its pore-forming domain into the cytoplasmic membrane. The common structural architecture of colicins comprises a translocation, a receptor-binding, and an activity domain. We have solved the crystal structure of colicin S4 to a resolution of 2.5 A, which shows a remarkably compact domain arrangement of four independent domains, including a unique domain duplication of the receptor-binding domain. Finally, we have determined the residues responsible for binding to the receptor OmpW by mutating exposed charged residues in one or both receptor-binding domains.
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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.