ArticleNature communications2020
Atomic structures of anthrax toxin protective antigen channels bound to partially unfolded lethal and edema factors.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- Step-by-step maturation mechanism of the binary toxin pore revealed by cryo-EM analysis.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Beyond the Static Caliper: Dynamical Translocases and the Mathematical Imperative for Single-Molecule Proteomics.bioRxiv : the preprint server for biology · 2026Article
- Structural basis for independent pore function of Vpb4 from Bacillus thuringiensis.Nature communications · 2026Article
- Rational Engineering of the Anthrax Toxin Nanopore Interface for Orthogonal Peptide Classification.ACS omega · 2026Article
- Structural basis for the assembly and translocation of the Vip1-Vip2 insecticidal toxin from Bacillus thuringiensis.Nature communications · 2026Article
- Peptide properties predict multistate translocation kinetics via protective antigen nanopores.Biophysical journal · 2026Article
- Dynamic gating by ϕ-clamp loop controls peptide translocation through the anthrax toxin nanopore.Biophysical journal · 2026Article
- A dynamical anthrax toxin nanopore biosensor for high-fidelity single-peptide classification.PLoS computational biology · 2026Article
- Review
- Pore Formation by Pore Forming Proteins in Lipid Membranes: Structural Insights Through Cryo-EM.The Journal of membrane biology · 2025Review
- Oligomerization of the Clostridioides difficile transferase B component proceeds through a stepwise mechanism.PLoS pathogens · 2025Article
- The N-terminus of themBio · 2025Article
- Determination of Dipicolinic Acid through the Antenna Effect of Eu(III) Coordination Polymer.Molecules (Basel, Switzerland) · 2024Article
- Repurposing FDA-approved disulfiram for targeted inhibition of diphtheria toxin and the binary protein toxins ofFrontiers in pharmacology · 2024Article
- Structural basis for calcium-stimulating pore formation of Vibrio α-hemolysin.Nature communications · 2023Article
- Gating of β-Barrel Protein Pores, Porins, and Channels: An Old Problem with New Facets.International journal of molecular sciences · 2023Review
- Cancer Drug Delivery Systems Using Bacterial Toxin Translocation Mechanisms.Bioengineering (Basel, Switzerland) · 2023Review
- Recombinant full-lengthFrontiers in immunology · 2022Article
- Single-particle cryo-EM reveals conformational variability of the oligomeric VCC β-barrel pore in a lipid bilayer.The Journal of cell biology · 2021Article
- Native structure of the RhopH complex, a key determinant of malaria parasite nutrient acquisition.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
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Authors and funding
6 authors.
Funding
Abstract
Following assembly, the anthrax protective antigen (PA) forms an oligomeric translocon that unfolds and translocates either its lethal factor (LF) or edema factor (EF) into the host cell. Here, we report the cryo-EM structures of heptameric PA channels with partially unfolded LF and EF at 4.6 and 3.1-Å resolution, respectively. The first α helix and β strand of LF and EF unfold and dock into a deep amphipathic cleft, called the α clamp, which resides at the interface of two PA monomers. The α-clamp-helix interactions exhibit structural plasticity when comparing the structures of lethal and edema toxins. EF undergoes a largescale conformational rearrangement when forming the complex with the channel. A critical loop in the PA binding interface is displaced for about 4 Å, leading to the weakening of the binding interface prior to translocation. These structures provide key insights into the molecular mechanisms of translocation-coupled protein unfolding and translocation.
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