Anthrax protective antigen

Function Anthrax protective antigen (PA) is the cell-binding part of the Bacillus anthracis anthrax toxin. The anthrax toxin is composed of the PA, lethal factor and edema factor. The PA translocates the lethal (LF) and edema factors (EF) into the cell. The 83kD form of PA (PA83) binds to the anthrax toxin receptor. A 20kD fragment (PA20) is cleaved off the PA83 and the remaining PA63 assembles into ring-shaped oligomer which becomes a membrane pre-channel. The PA pre-channel binds the lethal and edema factors allowing them to penetrate the membrane via pH gradient. For more details see Molecular Playground/Protective Antigen. Structural highlights PA contains 4 domains: is the N terminal (in yellow). It contains the furin protease cleavage site enabling the release of PA20. (in cyan) is the heptamerization domain of PA63. (in salmon) forms the heptameric pore with domain 2 and enabling LF and EF to penetrate the cell. (in magenta) is important for receptor recognition and pore formation.

spinqualitylabelsall models Anthrax protective antigen (PA83) complex with Ca+2 ions (PDB code 1acc) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

3D structures of anthrax protective antigen3D structures of anthrax protective antigen

Updated on 11-November-2015

{"openlevels":0}

• PA83
  • 1acc, 3tew, 3q8a, 3q8b, 4h2a – PA
    
  • 3tex, 3tey, 3tez, 3q8c, 3q8e, 4ee2, 4nam – PA (mutant)
    
  • 3mhz, 3q8f – PA with fluoro-histidine
    
  • 1t6b – PA + anthrax toxin receptor A/I domain
• PA63
  • 3hvd – PA63 (mutant)
    
  • 1tzo – PA63
    
  • 1tzn – PA63 + anthrax toxin receptor VWA domain
    
  • 3kwv – PA63 (mutant) + lethal factor
• PA domain 4
  • 3ino – PA domain 4
    
  • 3etb – PA domain 4 + antibody (mutant)