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Literature summary for 3.4.24.83 extracted from

  • Pentelute, B.L.; Barker, A.P.; Janowiak, B.E.; Kent, S.B.; Collier, R.J.
    A semisynthesis platform for investigating structure-function relationships in the N-terminal domain of the anthrax Lethal Factor (2010), ACS Chem. Biol., 5, 359-364.
    View publication on PubMedView publication on EuropePMC
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Application

Application Comment Organism
synthesis preparation of semisynthetic protective antigen-binding domain of anthrax lethal factor, LFN, by native chemical ligation of synthetic LFN residues 14-28 thioester with recombinant N29C-LFN residues 29-263 and comparison with two variants containing alterations in residues 14-28 of the N-terminal region. The properties of the variants in blocking ion conductance through the protective antigen pore and translocating across planar phospholipid bilayers in response to a pH gradient are consistent with current concepts of the mechanism of polypeptide translocation through the pore. The semisynthesis platform allows for investigation of the interaction of the pore with its substrates Bacillus anthracis

Protein Variants

Protein Variants Comment Organism
additional information preparation of semisynthetic protective antigen-binding domain of anthrax lethal factor, LFN, by native chemical ligation of synthetic LFN residues 14-28 thioester with recombinant N29C-LFN residues 29-263 and comparison with two variants containing alterations in residues 14-28 of the N-terminal region. An analogue with three positively charged residues and an acetylated N-terminus, blocks ion conductance more efficiently than the control analogue, which lacks charged residues in the N-terminal segment. The semisynthesis platform allows for investigation of the interaction of the pore with its substrates Bacillus anthracis

Organism

Organism UniProt Comment Textmining
Bacillus anthracis
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General Information

General Information Comment Organism
physiological function translocation of anthrax lethal factor protective antigen-binding domain LFN through the protective antigen pore is triggered by pH gradient. Residues 14-28 at the N-terminus of LFN are required for LFN to inhibit ion conductance through the pore. The translocation of substrate proteins through the protective antigen pore is dependent on the presence of both acidic and basic residues in the unstructured N-terminal region Bacillus anthracis