ArticleProtein science : a publication of the Protein Society2013
Three dimensional structure of the anthrax toxin translocon-lethal factor complex by cryo-electron microscopy.
Article in Protein science : a publication of the Protein Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- 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 structure of the fully-loaded asymmetric anthrax lethal toxin in its heptameric pre-pore state.PLoS pathogens · 2020Article
- Advances in cryoEM and its impact on β-pore forming proteins.Current opinion in structural biology · 2018Review
- Single-particle cryo-EM structure of a voltage-activated potassium channel in lipid nanodiscs.eLife · 2018Article
- Asymmetric Cryo-EM Structure of Anthrax Toxin Protective Antigen Pore with Lethal Factor N-Terminal Domain.Toxins · 2017Article
- Cell-free production of a functional oligomeric form of aThe Journal of biological chemistry · 2017Article
- Review
- A cell-free method for expressing and reconstituting membrane proteins enables functional characterization of the plant receptor-like protein kinase FERONIA.The Journal of biological chemistry · 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
- Direct Measurement of the Structure of Reconstituted High-Density Lipoproteins by Cryo-EM.Biophysical journal · 2016Article
- Conformational Chaperones for Structural Studies of Membrane Proteins Using Antibody Phage Display with Nanodiscs.Structure (London, England : 1993) · 2016Article
- Molecular assembly of lethal factor enzyme and pre-pore heptameric protective antigen in early stage of translocation.Journal of molecular modeling · 2016Article
- 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
- Detergent-free isolation, characterization, and functional reconstitution of a tetrameric K+ channel: the power of native nanodiscs.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- 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
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9 authors.
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Abstract
We have visualized by cryo-electron microscopy (cryo-EM) the complex of the anthrax protective antigen (PA) translocon and the N-terminal domain of anthrax lethal factor (LF(N) inserted into a nanodisc model lipid bilayer. We have determined the structure of this complex at a nominal resolution of 16 Å by single-particle analysis and three-dimensional reconstruction. Consistent with our previous analysis of negatively stained unliganded PA, the translocon comprises a globular structure (cap) separated from the nanodisc bilayer by a narrow stalk that terminates in a transmembrane channel (incompletely distinguished in this reconstruction). The globular cap is larger than the unliganded PA pore, probably due to distortions introduced in the previous negatively stained structures. The cap exhibits larger, more distinct radial protrusions, previously identified with PA domain three, fitted by elements of the NMFF PA prepore crystal structure. The presence of LF(N), though not distinguished due to the seven-fold averaging used in the reconstruction, contributes to the distinct protrusions on the cap rim volume distal to the membrane. Furthermore, the lumen of the cap region is less resolved than the unliganded negatively stained PA, due to the low contrast obtained in our images of this specimen. Presence of the LF(N) extended helix and N terminal unstructured regions may also contribute to this additional internal density within the interior of the cap. Initial NMFF fitting of the cryoEM-defined PA pore cap region positions the Phe clamp region of the PA pore translocon directly above an internal vestibule, consistent with its role in toxin translocation.
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