ArticleNature communications2021
Architecture of the outer-membrane core complex from a conjugative type IV secretion system.
Article in Nature communications, 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 17 papers.
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Who cites it
17 citing papers in PubMed.
- Type IV Secretion System Drives Lipid Mixing.bioRxiv : the preprint server for biology · 2026Article
- Type IV secretion systems: from structures to mechanisms.The EMBO journal · 2025Review
- The assembly of a hybrid type IV secretion system by a Crohn's disease-associated Escherichia coli strain.Nature communications · 2025Article
- OptimizedMicrobiology spectrum · 2025Article
- Not All Bacterial Outer-Membrane Proteins Are β-Barrels.microPublication biology · 2025Article
- Cryo-EM structure of a conjugative type IV secretion system suggests a molecular switch regulating pilus biogenesis.The EMBO journal · 2024Article
- Subdomains of theLife science alliance · 2024Article
- Chimeric systems composed of swapped Tra subunits between distantly-related F plasmids reveal striking plasticity among type IV secretion machines.PLoS genetics · 2024Article
- Structural and functional diversity of type IV secretion systems.Nature reviews. Microbiology · 2024Review
- Chimeric systems composed of swapped Tra subunits between distantly-related F plasmids reveal striking plasticity among type IV secretion machines.bioRxiv : the preprint server for biology · 2023Article
- Role of the CagY antenna projection inInfection and immunity · 2023Article
- DNA Transport through the Dynamic Type IV Secretion System.Infection and immunity · 2023Review
- The F-pilus biomechanical adaptability accelerates conjugative dissemination of antimicrobial resistance and biofilm formation.Nature communications · 2023Article
- Molecular architecture of bacterial type IV secretion systems.PLoS pathogens · 2022Review
- Contributions of F-specific subunits to the F plasmid-encoded type IV secretion system and F pilus.Molecular microbiology · 2022Article
- Functional comparison of anti-restriction and anti-methylation activities of ArdA, KlcA, and KlcAFrontiers in cellular and infection microbiology · 2022Article
- Article
Corrections and comments
- Erratum issued
Authors and funding
3 authors.
Funding
Abstract
Conjugation is one of the most important processes that bacteria utilize to spread antibiotic resistance genes among bacterial populations. Interbacterial DNA transfer requires a large double membrane-spanning nanomachine called the type 4 secretion system (T4SS) made up of the inner-membrane complex (IMC), the outer-membrane core complex (OMCC) and the conjugative pilus. The iconic F plasmid-encoded T4SS has been central in understanding conjugation for several decades, however atomic details of its structure are not known. Here, we report the structure of a complete conjugative OMCC encoded by the pED208 plasmid from E. coli, solved by cryo-electron microscopy at 3.3 Å resolution. This 2.1 MDa complex has a unique arrangement with two radial concentric rings, each having a different symmetry eventually contributing to remarkable differences in protein stoichiometry and flexibility in comparison to other OMCCs. Our structure suggests that F-OMCC is a highly dynamic complex, with implications for pilus extension and retraction during conjugation.
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