PA F427A (Anthrax Protective Mutant Antigen (PA F427A))
Dominant negative F427A protective antigen (PA) mutant that fails to translocate LF and EF. The F427 residue is in the lumen of the channel, where the ring of 7 or 8 F residues constitutes the “Psi clamp”, which is necessary for translocation of LF and EF polypeptides.
Anthrax toxin is a three-protein exotoxin secreted by virulent strains of the bacterium, Bacillus anthracis, the causative agent of anthrax. Anthrax toxin is composed of a cell-binding protein, known as protective antigen (PA), and two enzyme components, called edema factor (EF) and lethal factor (LF). Anthrax is caused by B. anthracis, a spore-forming, Gram positive, rod-shaped bacterium. The lethality of the disease is caused by the bacterium's two principal virulence factors: the polyglutamic acid capsule, which is anti-phagocytic, and the tripartite protein toxin, called anthrax toxin.
From the laboratory of Stephen H. Leppla, PhD, National Institute of Allergy and Infectious Diseases/NIH.
Dominant negative F427A protective antigen (PA) mutant that fails to translocate LF and EF. The F427 residue is in the lumen of the channel, where the ring of 7 or 8 F residues constitutes the “Psi clamp”, which is necessary for translocation of LF and EF polypeptides.
Anthrax toxin is a three-protein exotoxin secreted by virulent strains of the bacterium, Bacillus anthracis, the causative agent of anthrax. Anthrax toxin is composed of a cell-binding protein, known as protective antigen (PA), and two enzyme components, called edema factor (EF) and lethal factor (LF). Anthrax is caused by B. anthracis, a spore-forming, Gram positive, rod-shaped bacterium. The lethality of the disease is caused by the bacterium's two principal virulence factors: the polyglutamic acid capsule, which is anti-phagocytic, and the tripartite protein toxin, called anthrax toxin.
From the laboratory of Stephen H. Leppla, PhD, National Institute of Allergy and Infectious Diseases/NIH.
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| Product Type: | Protein |
| Name: | F427A |
| Alternative Name(s): | PA F427A |
| Accession ID: | P13423 |
| Strain: | Expressed in avirulent engineered B. anthracisstrain BH480 |
| Format: | Purified protein (liquid) |
| Purity: | Hydroxyapatite Chromatography |
| Buffer: | 10 mM HEPES pH 7.5, 0.50 mM EDTA |
| Concentration: | 2.23mg/mL |
| Storage: | -80C |
| Shipped: | Dry ice |
- Leppla SH. Production and purification of anthrax toxin. Methods Enzymol. 1988;165:103-16.
- Krantz, B. A., Melnyk, R. A., Zhang, S., Juris, S. J., Lacy, D. B., Wu, Z., Finkelstein, A., and Collier, R. J. (2005) A phenylalanine clamp catalyzes protein translocation through the anthrax toxin pore. Science 309, 777-781
- Sun, J., Lang, A. E., Aktories, K., and Collier, R. J. (2008) Phenylalanine-427 of anthrax protective antigen functions in both pore formation and protein translocation. Proc.Natl.Acad.Sci.U.S.A. 105, 4346-4351
- Bezrukov, S. M., Liu, X., Karginov, V. A., Wein, A. N., Leppla, S. H., Popoff, M. R., Barth, H., and Nestorovich, E. M. (2012) Interactions of high-affinity cationic blockers with the translocation pores of B. anthracis, C. botulinum, and C. perfringens binary toxins. Biophys.J. 103, 1208-1217
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