ArticleNature structural & molecular biology2008
GroEL as a molecular scaffold for structural analysis of the anthrax toxin pore.
Article in Nature structural & molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
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Who cites it
58 citing papers in PubMed.
- Challenges and approaches to studying pore-forming proteins.Biochemical Society transactions · 2021Review
- Advances in cryoEM and its impact on β-pore forming proteins.Current opinion in structural biology · 2018Review
- The Chaperonin GroEL: A Versatile Tool for Applied Biotechnology Platforms.Frontiers in molecular biosciences · 2018Article
- Laboratory evolution of artificially expanded DNA gives redesignable aptamers that target the toxic form of anthrax protective antigen.Nucleic acids research · 2016Article
- Chaperonin-Based Biolayer Interferometry To Assess the Kinetic Stability of Metastable, Aggregation-Prone Proteins.Biochemistry · 2016Article
- Roles of Anthrax Toxin Receptor 2 in Anthrax Toxin Membrane Insertion and Pore Formation.Toxins · 2016Review
- Folding of newly translated membrane protein CCR5 is assisted by the chaperonin GroEL-GroES.Scientific reports · 2015Article
- Ion selectivity of the anthrax toxin channel and its effect on protein translocation.The Journal of general physiology · 2015Article
- Following Natures Lead: On the Construction of Membrane-Inserted Toxins in Lipid Bilayer Nanodiscs.The Journal of membrane biology · 2015Article
- Ion conductance of the stem of the anthrax toxin channel during lethal factor translocation.Journal of molecular biology · 2015Article
- Article
- Review
- Cationic PAMAM dendrimers as pore-blocking binary toxin inhibitors.Biomacromolecules · 2014Article
- A protective antigen mutation increases the pH threshold of anthrax toxin receptor 2-mediated pore formation.Biochemistry · 2014Article
- Designing inhibitors of anthrax toxin.Expert opinion on drug discovery · 2014Review
- Monitoring the kinetics of the pH-driven transition of the anthrax toxin prepore to the pore by biolayer interferometry and surface plasmon resonance.Biochemistry · 2013Article
- Three dimensional structure of the anthrax toxin translocon-lethal factor complex by cryo-electron microscopy.Protein science : a publication of the Protein Society · 2013Article
- Recombinant GroEL enhances protective antigen-mediated protection against Bacillus anthracis spore challenge.Medical microbiology and immunology · 2013Article
- Assembly of anthrax toxin pore: lethal-factor complexes into lipid nanodiscs.Protein science : a publication of the Protein Society · 2013Article
- Biomphalysin, a new β pore-forming toxin involved in Biomphalaria glabrata immune defense against Schistosoma mansoni.PLoS pathogens · 2013Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
We analyzed the 440-kDa transmembrane pore formed by the protective antigen (PA) moiety of anthrax toxin in the presence of GroEL by negative-stain electron microscopy. GroEL binds both the heptameric PA prepore and the PA pore. The latter interaction retards aggregation of the pore, prolonging its insertion-competent state. Two populations of unaggregated pores were visible: GroEL-bound pores and unbound pores. This allowed two virtually identical structures to be reconstructed, at 25-A and 28-A resolution, respectively. The structures were mushroom-shaped objects with a 125-A-diameter cap and a 100-A-long stem, consistent with earlier biochemical data. Thus, GroEL provides a platform for obtaining initial glimpses of a membrane protein structure in the absence of lipids or detergents and can function as a scaffold for higher-resolution structural analysis of the PA pore.
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Registered trials
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.