Hemolysin: Difference between revisions

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{{STRUCTURE_7ahl|  PDB=7ahl | SIZE=400| SCENE= |right|CAPTION=α-hemolysin heptamer, [[7ahl]] }}
 
<StructureSection load='7ahl' size='350' side='right' caption='α-hemolysin heptamer (PDB code [[7ahl]]).' scene=''>
== Function ==
== Function ==
'''Hemolysin''' (HL) is exotoxin from bacteria which causes lysis of red blood cells<ref>PMID:20110774</ref>. 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.   
'''Hemolysin''' (HL) is exotoxin from bacteria which causes lysis of red blood cells<ref>PMID:20110774</ref>. 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.   
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== Relevance ==
== Relevance ==
HL acts as a virulence factor in the pathogenesis of invasive infections<ref>PMID:12564994</ref>.
HL acts as a virulence factor in the pathogenesis of invasive infections<ref>PMID:12564994</ref>.
 
</StructureSection>
== 3D Structures of hemolysin ==
== 3D Structures of hemolysin ==



Revision as of 09:09, 7 February 2017

α-hemolysin heptamer (PDB code 7ahl).

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3D Structures of hemolysin

Updated on 07-February-2017

A full page in Proteopedia exploring Toxins is found here.

  • 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

References