ArticleProceedings of the National Academy of Sciences of the United States of America2010
Three-dimensional structure of the anthrax toxin pore inserted into lipid nanodiscs and lipid vesicles.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
What it found
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Who cites it
60 citing papers in PubMed, 101 citations in OpenAlex.
- Structural basis for calcium-stimulating pore formation of Vibrio α-hemolysin.Nature communications · 2023Article
- Structure of the Human BK Ion Channel in Lipid Environment.Membranes · 2022Article
- Spectroscopic evidence of tetanus toxin translocation domain bilayer-induced refolding and insertion.Biophysical journal · 2021Article
- Anthrax toxin translocation complex reveals insight into the lethal factor unfolding and refolding mechanism.Scientific reports · 2021Article
- Crystallization of ApoA1 and ApoE4 nanolipoprotein particles and initial XFEL-based structural studies.Crystals · 2020Article
- Cryo-EM analysis of a membrane protein embedded in the liposome.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Atomic structures of anthrax toxin protective antigen channels bound to partially unfolded lethal and edema factors.Nature communications · 2020Article
- Cryo-EM sample preparation method for extremely low concentration liposomes.Ultramicroscopy · 2020Article
- Reconstitution and NMR Characterization of the Ion-Channel Accessory Subunit Barttin in Detergents and Lipid-Bilayer Nanodiscs.Frontiers in molecular biosciences · 2019Article
- Advances in cryoEM and its impact on β-pore forming proteins.Current opinion in structural biology · 2018Review
- Self-assembly of nanoscale particles with biosurfactants and membrane scaffold proteins.Biotechnology reports (Amsterdam, Netherlands) · 2017Article
- Asymmetric Cryo-EM Structure of Anthrax Toxin Protective Antigen Pore with Lethal Factor N-Terminal Domain.Toxins · 2017Article
- Enhanced imaging of lipid rich nanoparticles embedded in methylcellulose films for transmission electron microscopy using mixtures of heavy metals.Micron (Oxford, England : 1993) · 2017Article
- Nanodiscs in Membrane Biochemistry and Biophysics.Chemical reviews · 2017Review
- Antigenic characterization of the human immunodeficiency virus (HIV-1) envelope glycoprotein precursor incorporated into nanodiscs.PloS one · 2017Article
- Structure of anthrax lethal toxin prepore complex suggests a pathway for efficient cell entry.The Journal of general physiology · 2016Article
- Nanodiscs for structural and functional studies of membrane proteins.Nature structural & molecular biology · 2016Review
- Roles of Anthrax Toxin Receptor 2 in Anthrax Toxin Membrane Insertion and Pore Formation.Toxins · 2016Review
- The styrene-maleic acid copolymer: a versatile tool in membrane research.European biophysics journal : EBJ · 2016Review
- Controlled Co-reconstitution of Multiple Membrane Proteins in Lipid Bilayer Nanodiscs Using DNA as a Scaffold.ACS chemical biology · 2015Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
Abstract
A major goal in understanding the pathogenesis of the anthrax bacillus is to determine how the protective antigen (PA) pore mediates translocation of the enzymatic components of anthrax toxin across membranes. To obtain structural insights into this mechanism, we constructed PA-pore membrane complexes and visualized them by using negative-stain electron microscopy. Two populations of PA pores were visualized in membranes, vesicle-inserted and nanodisc-inserted, allowing us to reconstruct two virtually identical PA-pore structures at 22-A resolution. Reconstruction of a domain 4-truncated PA pore inserted into nanodiscs showed that this domain does not significantly influence pore structure. Normal mode flexible fitting of the x-ray crystallographic coordinates of the PA prepore indicated that a prominent flange observed within the pore lumen is formed by the convergence of mobile loops carrying Phe427, a residue known to catalyze protein translocation. Our results have identified the location of a crucial functional element of the PA pore and documented the value of combining nanodisc technology with electron microscopy to examine the structures of membrane-interactive proteins.
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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.