ArticleNature communications2019
Cryo-EM structures of the pore-forming A subunit from the Yersinia entomophaga ABC toxin.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Complete structures of the YenTc holotoxin prepore and pore reveal the evolutionary basis for chitinase incorporation into ABC toxins.Nature communications · 2025Article
- Article
- Evaluating TcAs for Use in Biotechnology Applications.Biotech (Basel (Switzerland)) · 2025Article
- Multistate kinetics of the syringe-like injection mechanism of Tc toxins.Science advances · 2025Article
- Review
- Biantennary N-glycans As Receptors for MARTX Toxins inbioRxiv : the preprint server for biology · 2024Article
- Article
- Yersinia entomophaga Tc toxin is released by T10SS-dependent lysis of specialized cell subpopulations.Nature microbiology · 2024Article
- Stepwise assembly and release of Tc toxins from Yersinia entomophaga.Nature microbiology · 2024Article
- Structures of the Insecticidal Toxin Complex Subunit XptA2 Highlight Roles for Flexible Domains.International journal of molecular sciences · 2023Article
- Gaining New Insights into Fundamental Biological Pathways by Bacterial Toxin-Based Genetic Screens.Bioengineering (Basel, Switzerland) · 2023Review
- Recent insights into mechanisms of cellular toxicity and cell recognition associated with the ABC family of pore-forming toxins.Biochemical Society transactions · 2023Article
- Article
- Membranes under the Magnetic Lens: A Dive into the Diverse World of Membrane Protein Structures Using Cryo-EM.Chemical reviews · 2022Review
- Mechanism of threonine ADP-ribosylation of F-actin by a Tc toxin.Nature communications · 2022Article
- Challenges and approaches to studying pore-forming proteins.Biochemical Society transactions · 2021Review
- Single-particle cryo-EM reveals conformational variability of the oligomeric VCC β-barrel pore in a lipid bilayer.The Journal of cell biology · 2021Article
- Identification of Diverse Toxin Complex Clusters and an eCIS Variant in Serratia proteamaculans Pathovars of the New Zealand Grass Grub (Microbiology spectrum · 2021Article
- Review
- Anthrax toxin translocation complex reveals insight into the lethal factor unfolding and refolding mechanism.Scientific reports · 2021Article
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Authors and funding
19 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
ABC toxins are pore-forming virulence factors produced by pathogenic bacteria. YenTcA is the pore-forming and membrane binding A subunit of the ABC toxin YenTc, produced by the insect pathogen Yersinia entomophaga. Here we present cryo-EM structures of YenTcA, purified from the native source. The soluble pre-pore structure, determined at an average resolution of 4.4 Å, reveals a pentameric assembly that in contrast to other characterised ABC toxins is formed by two TcA-like proteins (YenA1 and YenA2) and decorated by two endochitinases (Chi1 and Chi2). We also identify conformational changes that accompany membrane pore formation by visualising YenTcA inserted into liposomes. A clear outward rotation of the Chi1 subunits allows for access of the protruding translocation pore to the membrane. Our results highlight structural and functional diversity within the ABC toxin subfamily, explaining how different ABC toxins are capable of recognising diverse hosts.
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