Hemolysin

spinqualitylabelsall models α-hemolysin heptamer (PDB code 7ahl). Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function 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. Relevance HL acts as a virulence factor in the pathogenesis of invasive infections.

3D Printed Physical Model of Hemolysin

Shown below is a 3D printed physical model of Hemolysin. The model is shown in alpha carbon backbone format with each chain colored uniquely.

File:Hemolysin1 centerForBiomolecularModeling.jpg

The MSOE Center for BioMolecular Modeling

The MSOE Center for BioMolecular Modeling uses 3D printing technology to create physical models of protein and molecular structures, making the invisible molecular world more tangible and comprehensible. To view more protein structure models, visit our Model Gallery.

Updated on 20-April-2018

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• α-hemolysin
  • Pore forming toxin, α-hemolysin, Molecular Playground/ClyA – SaHL-α – Staphylococcus aureus
    

A full page in Proteopedia exploring Toxins is found here.

• • 3m2l, 3m4d, 4p24, 4yhd - 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, 5keh, 5kf3, 4w8q – PmHL A residues 30-265 – Proteus mirabilis
    
  • 5sz8, 5kkd, 4w8r, 4w8s, 4w8t - PmHL A residues 30-234 (mutant)
    
  • 1mt0 – EcHL B ATP-binding domain – Escherichia coli
    
  • 5c21, 5c22 - EcHL D residues 57-333
    
  • 2wcd – EcHL E residues 2-303 – Escherichia coli
    
  • 1qoy, 4pho, 4phq - EcHL E (mutant)
    
  • 2oai, 2r8d – HL corc_hlyc domain – Xylella fastidiosa
    
  • 2r2z – HL residues 346-435 – Enterococcus faecalis
    
  • 4wx3, 4wx5 - HL – Grimontia hollisae
    
• 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
    

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Mark Hoelzer, Wayne Decatur, Marius Mihasan, Alexander Berchansky