ArticleStructure (London, England : 1993)2004
Large-scale structural changes accompany binding of lethal factor to anthrax protective antigen: a cryo-electron microscopic study.
Article in Structure (London, England : 1993), 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 29 citations in OpenAlex.
- Solution Structures ofToxins · 2021Article
- Assembly and Function of the Anthrax Toxin Protein Translocation Complex.Sub-cellular biochemistry · 2021Review
- Cryo-EM structure of the fully-loaded asymmetric anthrax lethal toxin in its heptameric pre-pore state.PLoS pathogens · 2020Article
- Structure of anthrax lethal toxin prepore complex suggests a pathway for efficient cell entry.The Journal of general physiology · 2016Article
- Molecular assembly of lethal factor enzyme and pre-pore heptameric protective antigen in early stage of translocation.Journal of molecular modeling · 2016Article
- Optimized negative-staining electron microscopy for lipoprotein studies.Biochimica et biophysica acta · 2013Review
- Anthrax toxin protective antigen--insights into molecular switching from prepore to pore.Protein science : a publication of the Protein Society · 2012Review
- Anthrax toxin-neutralizing antibody reconfigures the protective antigen heptamer into a supercomplex.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Anthrax edema toxin induces maturation of dendritic cells and enhances chemotaxis towards macrophage inflammatory protein 3beta.Infection and immunity · 2009Article
- Paratope diversity in the human antibody response to Bacillus anthracis protective antigen.Molecular immunology · 2008Article
- Cryo-electron microscopy study of bacteriophage T4 displaying anthrax toxin proteins.Virology · 2007Article
- Model of the toxic complex of anthrax: responsive conformational changes in both the lethal factor and the protective antigen heptamer.Protein science : a publication of the Protein Society · 2006Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
Anthrax toxin (AT), secreted by Bacillus anthracis, is a three-protein cocktail of lethal factor (LF, 90 kDa), edema factor (EF, 89 kDa), and the protective antigen (PA, 83 kDa). Steps in anthrax toxicity involve (1) binding of ligand (EF/LF) to a heptamer of PA63 (PA63h) generated after N-terminal proteolytic cleavage of PA and, (2) following endocytosis of the complex, translocation of the ligand into the cytosol by an as yet unknown mechanism. The PA63h.LF complex was directly visualized from analysis of images of specimens suspended in vitrified buffer by cryo-electron microscopy, which revealed that the LF molecule, localized to the nonmembrane-interacting face of the oligomer, interacts with four successive PA63 monomers and partially unravels the heptamer, thereby widening the central lumen. The observed structural reorganization in PA63h likely facilitates the passage of the large 90 kDa LF molecule through the lumen en route to its eventual delivery across the membrane bilayer.
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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.