Hemolysin: Difference between revisions

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<StructureSection load='7ahl' size='350' side='right' caption='α-hemolysin heptamer (PDB code [[7ahl]]).' scene=''>
<StructureSection load='7ahl' size='350' side='right' caption='α-hemolysin heptamer (PDB code [[7ahl]]).' scene=''>
== Function ==
== Function ==
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**[[3anz]], [[7ahl]] – SaHL-α – ''Staphylococcus aureus''<br />
**[[3anz]], [[7ahl]] – SaHL-α – ''Staphylococcus aureus''<br />
A full page in Proteopedia exploring [[7ahl]] is found [[Pore_forming_toxin,_α-hemolsyin|here]].<br/>
A full page in Proteopedia exploring [[7ahl]] is found [[Pore_forming_toxin,_α-hemolsyin|here]].<br/>
**[[3m2l]], [[3m4d]], [[4p24]] - SaHL-α (mutant)<br />
**[[3m2l]], [[3m4d]], [[4p24]], [[4yhd]] - SaHL-α (mutant)<br />
**[[3m3r]], [[3m4e]] - SaHL-α (mutant) + β-cyclodextrin<br />
**[[3m3r]], [[3m4e]] - SaHL-α (mutant) + β-cyclodextrin<br />
**[[4idj]], [[4u6v]] - SaHL-α + antibody<br />
**[[4idj]], [[4u6v]] - SaHL-α + antibody<br />
Line 49: Line 48:
**[[3a57]] – HL 2 – ''Vibrio parahaemolyticus''<br />
**[[3a57]] – HL 2 – ''Vibrio parahaemolyticus''<br />
**[[3hvn]] – HL (mutant) – ''Streptococcus suis''<br />
**[[3hvn]] – HL (mutant) – ''Streptococcus suis''<br />
**[[3fy3]] – HL A residues 30-265 – ''Proteus mirabilis''<br />
**[[3fy3]], [[5keh]], [[5kf3]], [[4w8q]] – PmHL A residues 30-265 – ''Proteus mirabilis''<br />
**[[5sz8]], [[5kkd]], [[4w8r]], [[4w8s]], [[4w8t]] - PmHL A residues 30-234 (mutant)<br />
**[[1mt0]] – EcHL B ATP-binding domain – ''Escherichia coli''<br />
**[[5c21]], [[5c22]] - EcHL D residues 57-333 <br />
**[[2wcd]] – EcHL E residues 2-303 – ''Escherichia coli''<br />
**[[2wcd]] – EcHL E residues 2-303 – ''Escherichia coli''<br />
**[[1qoy]], [[4pho]], [[4phq]] - EcHL E (mutant)<br />
**[[1qoy]], [[4pho]], [[4phq]] - EcHL E (mutant)<br />
**[[1mt0]] – EcHL B ATP-binding domain<br />
**[[2oai]], [[2r8d]] – HL corc_hlyc domain – ''Xylella fastidiosa''<br />
**[[2oai]], [[2r8d]] – HL corc_hlyc domain – ''Xylella fastidiosa''<br />
**[[2r2z]] – HL residues 346-435 – ''Enterococcus faecalis''<br />
**[[2r2z]] – HL residues 346-435 – ''Enterococcus faecalis''<br />
**[[4wx3]], [[4wx5]] - HL – ''Grimontia hollisae''<br />


*Alpha-toxin
*Alpha-toxin

Revision as of 11:16, 12 June 2017

Function

Hemolysin (HL) is exotoxin from bacteria which causes lysis of red blood cells[1]. 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[2].

α-hemolysin heptamer (PDB code 7ahl).

Drag the structure with the mouse to rotate

3D Structures of hemolysin3D Structures of hemolysin

Updated on 12-June-2017

A full page in Proteopedia exploring 7ahl 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, 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

ReferencesReferences

  1. Mestre MB, Fader CM, Sola C, Colombo MI. Alpha-hemolysin is required for the activation of the autophagic pathway in Staphylococcus aureus-infected cells. Autophagy. 2010 Jan;6(1):110-25. PMID:20110774
  2. Nizet V. Streptococcal beta-hemolysins: genetics and role in disease pathogenesis. Trends Microbiol. 2002 Dec;10(12):575-80. PMID:12564994

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Wayne Decatur, Alexander Berchansky, Michal Harel, Mark Hoelzer