ArticleThe EMBO journal2013
Structure of a bacterial type IV secretion core complex at subnanometre resolution.
Article in The EMBO journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed.
- Repurposing the bacterial surface display technology for drug delivery.Advanced drug delivery reviews · 2025Review
- The Potential Roles of Prophages in the Pathogenicity ofAntibiotics (Basel, Switzerland) · 2025Article
- The type IV secretion system ofMicrobial genomics · 2025Article
- Structural and functional diversity of type IV secretion systems.Nature reviews. Microbiology · 2024Review
- Structural Analysis of Protein Complexes by Cryo-Electron Microscopy.Methods in molecular biology (Clifton, N.J.) · 2024Review
- Role of the CagY antenna projection inInfection and immunity · 2023Article
- Article
- DNA Transport through the Dynamic Type IV Secretion System.Infection and immunity · 2023Review
- Molecular architecture of bacterial type IV secretion systems.PLoS pathogens · 2022Review
- Article
- Architecture of the outer-membrane core complex from a conjugative type IV secretion system.Nature communications · 2021Article
- Secretion of Pertussis Toxin fromToxins · 2021Review
- Type IV secretion systems: Advances in structure, function, and activation.Molecular microbiology · 2021Review
- Structural analysis of theeLife · 2020Article
- Genomic analysis of 40 prophages located in the genomes of 16 carbapenemase-producing clinical strains ofMicrobial genomics · 2020Article
- Article
- Article
- Inhibiting bacterial secretion systems in the fight against antibiotic resistance.MedChemComm · 2019Review
- From conjugation to T4S systems in Gram-negative bacteria: a mechanistic biology perspective.EMBO reports · 2019Review
- Bacteria-Killing Type IV Secretion Systems.Frontiers in microbiology · 2019Review
Corrections and comments
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Authors and funding
11 authors.
Funding
Abstract
Type IV secretion (T4S) systems are able to transport DNAs and/or proteins through the membranes of bacteria. They form large multiprotein complexes consisting of 12 proteins termed VirB1-11 and VirD4. VirB7, 9 and 10 assemble into a 1.07 MegaDalton membrane-spanning core complex (CC), around which all other components assemble. This complex is made of two parts, the O-layer inserted in the outer membrane and the I-layer inserted in the inner membrane. While the structure of the O-layer has been solved by X-ray crystallography, there is no detailed structural information on the I-layer. Using high-resolution cryo-electron microscopy and molecular modelling combined with biochemical approaches, we determined the I-layer structure and located its various components in the electron density. Our results provide new structural insights on the CC, from which the essential features of T4S system mechanisms can be derived.
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