ArticleProceedings of the National Academy of Sciences of the United States of America2016
Peptide- and proton-driven allosteric clamps catalyze anthrax toxin translocation across membranes.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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22 citing papers in PubMed, 22 citations in OpenAlex.
- 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
- Single-molecule sensing with an anthrax nanopore enabled by pH-asymmetric ionic liquids.Journal of nanobiotechnology · 2025Article
- Deep learning-based classification of peptide analytes from single-channel nanopore translocation events.PloS one · 2025Article
- α-Synuclein kinetically regulates the nascent fusion pore dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Anthrax toxin translocation complex reveals insight into the lethal factor unfolding and refolding mechanism.Scientific reports · 2021Article
- Site-Specific Labeling andBiochemistry · 2021Article
- Intein-mediated cytoplasmic reconstitution of a split toxin enables selective cell ablation in mixed populations and tumor xenografts.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Cryo-EM structures reveal translocational unfolding in the clostridial binary iota toxin complex.Nature structural & molecular biology · 2020Article
- Atomic structures of anthrax toxin protective antigen channels bound to partially unfolded lethal and edema factors.Nature communications · 2020Article
- Resolving kinetic intermediates during the regulated assembly and disassembly of fusion pores.Nature communications · 2020Article
- Real-Time Nanopore-Based Recognition of Protein Translocation Success.Biophysical journal · 2018Article
- Effect of endosomal acidification on small ion transport through the anthrax toxin PAFEBS letters · 2017Article
- The Impact of Protonation on Early Translocation of Anthrax Lethal Factor: Kinetics from Molecular Dynamics Simulations and Milestoning Theory.Journal of the American Chemical Society · 2017Article
- Reply to Yamini and Nestorovich: Alternate clamped states of the anthrax toxin protective antigen channel.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
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2 authors at 1 institution in 1 country.
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Abstract
Anthrax toxin is an intracellularly acting toxin in which sufficient information is available regarding the structure of its transmembrane channel, allowing for detailed investigation of models of translocation. Anthrax toxin, comprising three proteins-protective antigen (PA), lethal factor (LF), and edema factor-translocates large proteins across membranes. Here we show that the PA translocase channel has a transport function in which its catalytic active sites operate allosterically. We find that the phenylalanine clamp (ϕ-clamp), the known conductance bottleneck in the PA translocase, gates as either a more closed state or a more dilated state. Thermodynamically, the two channel states have >300-fold different binding affinities for an LF-derived peptide. The change in clamp thermodynamics requires distant α-clamp and ϕ-clamp sites. Clamp allostery and translocation are more optimal for LF peptides with uniform stereochemistry, where the least allosteric and least efficiently translocated peptide had a mixed stereochemistry. Overall, the kinetic results are in less agreement with an extended-chain Brownian ratchet model but, instead, are more consistent with an allosteric helix-compression model that is dependent also on substrate peptide coil-to-helix/helix-to-coil cooperativity.
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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.