ArticleNature communications2018
Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB.
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.
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Who cites it
34 citing papers in PubMed.
- Cryo-EM structure of detergent-boundbioRxiv : the preprint server for biology · 2026Article
- Purification and Oligomerization of YaxAB Nanopores.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Pore Formation by Pore Forming Proteins in Lipid Membranes: Structural Insights Through Cryo-EM.The Journal of membrane biology · 2025Review
- Nanopores with an Engineered Selective Entropic Gate Detect Proteins at Nanomolar Concentration in Complex Biological Sample.Journal of the American Chemical Society · 2025Article
- Nanopore-Functionalized Hybrid Lipid-Block Copolymer Membranes Allow Efficient Single-Molecule Sampling and Stable Sensing of Human Serum.Advanced materials (Deerfield Beach, Fla.) · 2025Article
- Article
- Story of Pore-Forming Proteins from Deadly Disease-Causing Agents to Modern Applications with Evolutionary Significance.Molecular biotechnology · 2024Review
- Structure of theProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Protein Sizing with 15 nm Conical Biological Nanopore YaxAB.ACS nano · 2023Article
- A coiled-coil-based design strategy for the thermostabilization of G-protein-coupled receptors.Scientific reports · 2023Article
- Single-molecule fingerprinting of protein-drug interaction using a funneled biological nanopore.Nature communications · 2023Article
- A Genomic Island of Vibrio cholerae Encodes a Three-Component Cytotoxin with Monomer and Protomer Forms Structurally Similar to Alpha-Pore-Forming Toxins.Journal of bacteriology · 2022Article
- Bacterial pore-forming toxins.Microbiology (Reading, England) · 2022Article
- Article
- Toxigenic Properties ofToxins · 2022Review
- Single-particle cryo-EM reveals conformational variability of the oligomeric VCC β-barrel pore in a lipid bilayer.The Journal of cell biology · 2021Article
- A tripartite cytolytic toxin formed byProceedings of the National Academy of Sciences of the United States of America · 2021Article
- FALCON2: a web server for high-quality prediction of protein tertiary structures.BMC bioinformatics · 2021Article
- Beyond pore formation: reorganization of the plasma membrane induced by pore-forming proteins.Cellular and molecular life sciences : CMLS · 2021Review
- Cryo-EM structures of an insecticidal Bt toxin reveal its mechanism of action on the membrane.Nature communications · 2021Article
Corrections and comments
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pore-forming toxins (PFT) are virulence factors that transform from soluble to membrane-bound states. The Yersinia YaxAB system represents a family of binary α-PFTs with orthologues in human, insect, and plant pathogens, with unknown structures. YaxAB was shown to be cytotoxic and likely involved in pathogenesis, though the molecular basis for its two-component lytic mechanism remains elusive. Here, we present crystal structures of YaxA and YaxB, together with a cryo-electron microscopy map of the YaxAB complex. Our structures reveal a pore predominantly composed of decamers of YaxA-YaxB heterodimers. Both subunits bear membrane-active moieties, but only YaxA is capable of binding to membranes by itself. YaxB can subsequently be recruited to membrane-associated YaxA and induced to present its lytic transmembrane helices. Pore formation can progress by further oligomerization of YaxA-YaxB dimers. Our results allow for a comparison between pore assemblies belonging to the wider ClyA-like family of α-PFTs, highlighting diverse pore architectures.
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