ArticleNature2018
Tc toxin activation requires unfolding and refolding of a β-propeller.
Article in Nature, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
What it found
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Who cites it
35 citing papers in PubMed.
- Ancestral neuronal receptors are bacterial accessory toxins.Nature communications · 2026Article
- Complete structures of the YenTc holotoxin prepore and pore reveal the evolutionary basis for chitinase incorporation into ABC toxins.Nature communications · 2025Article
- Genomic characterization ofMicrobial genomics · 2025Article
- Structural basis of Fusobacterium nucleatum adhesin Fap2 interaction with receptors on cancer and immune cells.Nature communications · 2025Article
- 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
- Thioredoxin 1 moonlights as a chaperone for an interbacterial ADP-ribosyltransferase toxin.Nature communications · 2024Article
- Review
- 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
- Structure and activation mechanism of the Makes caterpillars floppy 1 toxin.Nature communications · 2023Article
- Structures of the Insecticidal Toxin Complex Subunit XptA2 Highlight Roles for Flexible Domains.International journal of molecular sciences · 2023Article
- Regulation and Functionality of a Holin/Endolysin Pair Involved in Killing of Galleria mellonella and Caenorhabditis elegans by Yersinia enterocolitica.Applied and environmental microbiology · 2023Article
- Recent insights into mechanisms of cellular toxicity and cell recognition associated with the ABC family of pore-forming toxins.Biochemical Society transactions · 2023Article
- TomoTwin: generalized 3D localization of macromolecules in cryo-electron tomograms with structural data mining.Nature methods · 2023Article
- Native structure of mosquito salivary protein uncovers domains relevant to pathogen transmission.Nature communications · 2023Article
- Genetic Engineering ofAccess microbiology · 2023Article
- Article
- Insecticidal Activity of Chitinases fromToxins · 2022Article
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tc toxins secrete toxic enzymes into host cells using a unique syringe-like injection mechanism. They are composed of three subunits, TcA, TcB and TcC. TcA forms the translocation channel and the TcB-TcC heterodimer functions as a cocoon that shields the toxic enzyme. Binding of the cocoon to the channel triggers opening of the cocoon and translocation of the toxic enzyme into the channel. Here we show in atomic detail how the assembly of the three components activates the toxin. We find that part of the cocoon completely unfolds and refolds into an alternative conformation upon binding. The presence of the toxic enzyme inside the cocoon is essential for its subnanomolar binding affinity for the TcA subunit. The enzyme passes through a narrow negatively charged constriction site inside the cocoon, probably acting as an extruder that releases the unfolded protein with its C terminus first into the translocation channel.
Indexed as
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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.