ArticleBiochemistry2011
Cys-Cys cross-linking shows contact between the N-terminus of lethal factor and Phe427 of the anthrax toxin pore.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed, 10 citations in OpenAlex.
- Engineered Cross-Linking to Study the Pore Architecture of the CRAC Channel.Methods in molecular biology (Clifton, N.J.) · 2018Article
- Asymmetric Cryo-EM Structure of Anthrax Toxin Protective Antigen Pore with Lethal Factor N-Terminal Domain.Toxins · 2017Article
- Following Natures Lead: On the Construction of Membrane-Inserted Toxins in Lipid Bilayer Nanodiscs.The Journal of membrane biology · 2015Article
- Three dimensional structure of the anthrax toxin translocon-lethal factor complex by cryo-electron microscopy.Protein science : a publication of the Protein Society · 2013Article
- Assembly of anthrax toxin pore: lethal-factor complexes into lipid nanodiscs.Protein science : a publication of the Protein Society · 2013Article
- Obstructing toxin pathways by targeted pore blockage.Chemical reviews · 2012Review
- Bacillus anthracis edema factor substrate specificity: evidence for new modes of action.Toxins · 2012Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Electrophysiological studies of wild-type and mutated forms of anthrax protective antigen (PA) suggest that the Phe clamp, a structure formed by the Phe427 residues within the lumen of the oligomeric PA pore, binds the unstructured N-terminus of the lethal factor and the edema factor during initiation of translocation. We now show by electrophysiological measurements and gel shift assays that a single Cys introduced into the Phe clamp can form a disulfide bond with a Cys placed at the N-terminus of the isolated N-terminal domain of LF. These results demonstrate direct contact of these Cys residues, supporting a model in which the interaction of the unstructured N-terminus of the translocated moieties with the Phe clamp initiates N- to C-terminal threading of these moieties through the 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.