ArticleNature communications2018
Structure of the type VI secretion system TssK-TssF-TssG baseplate subcomplex revealed by cryo-electron microscopy.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
What it found
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Who cites it
34 citing papers in PubMed.
- The Lord of the Rings: Cysteine bonds crosslink the tail of siphovirus.Protein science : a publication of the Protein Society · 2026Article
- Conformational changes of the baseplate regulating tail contraction of Staphylococcus phage 812.The EMBO journal · 2026Article
- Crystal structure of the type VI secretion system adaptor protein Tla3 from Pseudomonas aeruginosa.Acta crystallographica. Section F, Structural biology communications · 2026Article
- Tvp complexes support formation of the VgrG-PAAR spike during Type VI secretion system assembly.The EMBO journal · 2026Article
- An ubiquitous antibacterial toxin from human gut bacteria engenders neonatal colonization advantage.Nature communications · 2026Article
- Stepwise firing mechanism of an extracellular contractile injection system.Nature communications · 2026Article
- TseCurrent research in microbial sciences · 2026Article
- From past to present: the crosstalk between type VI secretion system of Salmonella and host.Archives of microbiology · 2025Review
- The Competitive Edge: T6SS-Mediated Interference Competition byMicroorganisms · 2025Review
- Not just passengers: effectors contribute to the assembly of the type VI secretion system as structural building blocks.Journal of bacteriology · 2025Review
- The Tol Pal system integrates maintenance of the three layered cell envelope.npj antimicrobials and resistance · 2024Review
- Type VI secretion systems promote intraspecific competition and host interactions in a bee gut symbiont.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- The role of type VI secretion system genes in antibiotic resistance and virulence inFrontiers in cellular and infection microbiology · 2024Article
- Distribution and diversity of type VI secretion system clusters inMicrobial genomics · 2023Article
- The role of integration host factor in biofilm and virulence of high-alcohol-producingMicrobiology spectrum · 2023Article
- Article
- Killing in the name of: T6SS structure and effector diversity.Microbiology (Reading, England) · 2023Review
- The type-VI secretion system of the beneficial symbiontMicrobiology (Reading, England) · 2023Review
- Uncovering the Secretion Systems ofAntibiotics (Basel, Switzerland) · 2023Review
- Activity and Crystal Structure of the Adherent-InvasiveInternational journal of molecular sciences · 2023Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Type VI secretion systems (T6SSs) translocate effectors into target cells and are made of a contractile sheath and a tube docked onto a multi-protein transmembrane complex via a baseplate. Although some information is available about the mechanisms of tail contraction leading to effector delivery, the detailed architecture and function of the baseplate remain unknown. Here, we report the 3.7 Å resolution cryo-electron microscopy reconstruction of an enteroaggregative Escherichia coli baseplate subcomplex assembled from TssK, TssF and TssG. The structure reveals two TssK trimers interact with a locally pseudo-3-fold symmetrical complex comprising two copies of TssF and one copy of TssG. TssF and TssG are structurally related to each other and to components of the phage T4 baseplate and of the type IV secretion system, strengthening the evolutionary relationships among these macromolecular machines. These results, together with bacterial two-hybrid assays, provide a structural framework to understand the T6SS baseplate architecture.
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