Hemolysin

Hemolysin (HL) is exotoxin from bacteria which causes lysis of red blood cells. Hemolysin from the bacterium Clostridium are called alpha-toxin (AT). AT is a zinc metalloenzyme and binds to the membrane in the presence of calcium. It acts as a phospholipase C.

See details for α-hemolysin in Pore forming toxin, α-hemolysin. See details of hemolysin E in Molecular Playground/ClyA.

For toxins in Proteopdia see Toxins.

3D Structures of hemolysin3D Structures of hemolysin

Updated on 29-October-2015

{"openlevels":0}

• α-hemolysin
  • 3anz, 7ahl – SaHL-α – Staphylococcus aureus
    

A full page in Proteopedia exploring 7ahl is found here.

• • 3m2l, 3m4d, 4p24 - SaHL-α (mutant)
    
  • 3m3r, 3m4e - SaHL-α (mutant) + β-cyclodextrin
    
  • 4idj, 4u6v - SaHL-α + antibody
    
• β-hemolysin
  • 3k55 – SaHL-β)
    
  • 3i5v - SaHL-β residues 35-330)
    
  • 3i41 - SaHL-β residues 35-330 (mutant)
    
  • 3i46, 3i48 - SaHL-β residues 35-330 (mutant)
    + metal ion
• γ-hemolysin
  • 2qk7 – SaHL-γ component A (mutant) +B (mutant)
    
  • 3b07 - SaHL-γ component A+B
    
  • 4p1x - SaHL-γ component B (mutant)+C
    
  • 4p1y - SaHL-γ component A + B (mutant)
    
• δ-hemolysin
  • 2kam – SaHL-δ - NMR
• Hemolysin
  • 3o44 – VcHL residues 161-741 – Vibrio cholerae
    
  • 1xez – VcHL (mutant)
    
  • 3a57 – HL 2 – Vibrio parahaemolyticus
    
  • 3hvn – HL (mutant) – Streptococcus suis
    
  • 3fy3 – HL A residues 30-265 – Proteus mirabilis
    
  • 2wcd – EcHL E residues 2-303 – Escherichia coli
    
  • 1qoy, 4pho, 4phq - EcHL E (mutant)
    
  • 1mt0 – EcHL B ATP-binding domain
    
  • 2oai, 2r8d – HL corc_hlyc domain – Xylella fastidiosa
    
  • 2r2z – HL residues 346-435 – Enterococcus faecalis
    
• Alpha-toxin
  • 2wxt, 1ca1 - CpAT + Cd + Zn – Clostridium perfringens
    
  • 1qm6, 1gyg, 1kho - CpAT + Zn
    
  • 2wy6, 2wxu – CpAT (mutant) + Ca + Cd + Zn
    
  • 1qmd - CpAT + Ca + Zn
    
  • 1olp - AT + Ca + Zn – Clostridium absonum
    
  • 2vk9 - AT – Clostridium novyi