ArticleProceedings of the National Academy of Sciences of the United States of America2019
Structure of a Tc holotoxin pore provides insights into the translocation mechanism.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 41 citations in OpenAlex.
- Complete structures of the YenTc holotoxin prepore and pore reveal the evolutionary basis for chitinase incorporation into ABC toxins.Nature communications · 2025Article
- Transcriptomic insights into the resistance mechanism of Penaeus vannamei against highly lethal Vibrio parahaemolyticus.Scientific reports · 2025Article
- Structural basis for immune cell binding ofProceedings of the National Academy of Sciences of the United States of America · 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
- Review
- Article
- Yersinia entomophaga Tc toxin is released by T10SS-dependent lysis of specialized cell subpopulations.Nature microbiology · 2024Article
- 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
- Structural changes upon membrane insertion of the insecticidal pore-forming toxins produced byFrontiers in insect science · 2023Review
- 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
- Article
- N-terminal signal peptides facilitate the engineering of PVC complex as a potent protein delivery system.Science advances · 2022Article
- The life cycle-dependent transcriptional profile of the obligate intracellular amoeba symbiont Amoebophilus asiaticus.FEMS microbiology ecology · 2022Article
- Accelerated 2D Classification With ISAC Using GPUs.Frontiers in molecular biosciences · 2022Article
- Challenges and approaches to studying pore-forming proteins.Biochemical Society transactions · 2021Review
- Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tc toxins are modular toxin systems of insect and human pathogenic bacteria. They are composed of a 1.4-MDa pentameric membrane translocator (TcA) and a 250-kDa cocoon (TcB and TcC) encapsulating the 30-kDa toxic enzyme (C terminus of TcC). Binding of Tc toxins to target cells and a pH shift trigger the conformational transition from the soluble prepore state to the membrane-embedded pore. Subsequently, the toxic enzyme is translocated and released into the cytoplasm. A high-resolution structure of a holotoxin embedded in membranes is missing, leaving open the question of whether TcB-TcC has an influence on the conformational transition of TcA. Here we show in atomic detail a fully assembled 1.7-MDa Tc holotoxin complex from
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