Hemolysin

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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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'''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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'''Hemolysin''' (HL) is exotoxin from bacteria which causes lysis of red blood cells<ref>PMID:20110774</ref>.
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*'''alpha-hemolysin''' is a transmembrane pore-forming heptameric molecule<ref>PMID:8943190</ref>. See details for in [[Pore forming toxin, α-hemolysin]].
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*'''delta-hemolysin''' is a 26 amino acid peptide from the bacterium ''Staphylococcus'' exhibiting antimicrobial activity against'' Legionerlla'' <ref>PMID:19150639</ref>.
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See details for α-hemolysin in [[Pore forming toxin, α-hemolysin]].
 
See details of hemolysin E in [[Molecular Playground/ClyA]].
See details of hemolysin E in [[Molecular Playground/ClyA]].
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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>.
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</StructureSection>
 
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== 3D Structures of hemolysin ==
 
==3D Printed Physical Model of Hemolysin==
==3D Printed Physical Model of Hemolysin==
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Shown below is a 3D printed physical model of Hemolysin. The model is shown in alpha carbon backbone format with each chain colored uniquely.
Shown below is a 3D printed physical model of Hemolysin. The model is shown in alpha carbon backbone format with each chain colored uniquely.
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[[Image:hemolysin1_centerForBiomolecularModeling.jpg]]
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[[Image:hemolysin1_centerForBioMolecularModeling.jpg|550px]]
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[[Image:hemolysin2_centerForBioMolecularModeling.jpg]]
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[[Image:hemolysin2_centerForBioMolecularModeling.jpg|550px]]
====The MSOE Center for BioMolecular Modeling====
====The MSOE Center for BioMolecular Modeling====
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The [http://cbm.msoe.edu 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 [http://cbm.msoe.edu/educationalmedia/modelgallery/ Model Gallery].
The [http://cbm.msoe.edu 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 [http://cbm.msoe.edu/educationalmedia/modelgallery/ Model Gallery].
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== 3D Structures of hemolysin ==
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[[Hemolysin 3D structures]]
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</StructureSection>
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
 
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{{#tree:id=OrganizedByTopic|openlevels=0|
 
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*α-hemolysin
 
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**[[3anz]], [[7ahl]] – SaHL-α – ''Staphylococcus aureus''<br />
 
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A full page in Proteopedia exploring [[7ahl]] is found [[Pore_forming_toxin,_α-hemolsyin|here]].<br/>
 
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**[[3m2l]], [[3m4d]], [[4p24]], [[4yhd]] - SaHL-α (mutant)<br />
 
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**[[3m3r]], [[3m4e]] - SaHL-α (mutant) + β-cyclodextrin<br />
 
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**[[4idj]], [[4u6v]] - SaHL-α + antibody<br />
 
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*β-hemolysin
 
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**[[3k55]] – SaHL-β)<br />
 
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**[[3i5v]] - SaHL-β residues 35-330)<br />
 
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**[[3i41]] - SaHL-β residues 35-330 (mutant)<br />
 
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**[[3i46]], [[3i48]] - SaHL-β residues 35-330 (mutant)<br /> + metal ion
 
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*γ-hemolysin
 
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**[[2qk7]] – SaHL-γ component A (mutant) +B (mutant)<br />
 
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**[[3b07]] - SaHL-γ component A+B<br />
 
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**[[4p1x]] - SaHL-γ component B (mutant)+C<br />
 
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**[[4p1y]] - SaHL-γ component A + B (mutant)<br />
 
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*δ-hemolysin
 
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**[[2kam]] – SaHL-δ - NMR
 
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*Hemolysin
 
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**[[3o44]] – VcHL residues 161-741 – ''Vibrio cholerae''<br />
 
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**[[1xez]] – VcHL (mutant)<br />
 
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**[[3a57]] – HL 2 – ''Vibrio parahaemolyticus''<br />
 
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**[[3hvn]] – HL (mutant) – ''Streptococcus suis''<br />
 
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**[[3fy3]], [[5keh]], [[5kf3]], [[4w8q]] – PmHL A residues 30-265 – ''Proteus mirabilis''<br />
 
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**[[5sz8]], [[5kkd]], [[4w8r]], [[4w8s]], [[4w8t]] - PmHL A residues 30-234 (mutant)<br />
 
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**[[1mt0]] – EcHL B ATP-binding domain – ''Escherichia coli''<br />
 
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**[[5c21]], [[5c22]] - EcHL D residues 57-333 <br />
 
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**[[2wcd]] – EcHL E residues 2-303 – ''Escherichia coli''<br />
 
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**[[1qoy]], [[4pho]], [[4phq]] - EcHL E (mutant)<br />
 
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**[[2oai]], [[2r8d]] – HL corc_hlyc domain – ''Xylella fastidiosa''<br />
 
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**[[2r2z]] – HL residues 346-435 – ''Enterococcus faecalis''<br />
 
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**[[4wx3]], [[4wx5]] - HL – ''Grimontia hollisae''<br />
 
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*Alpha-toxin
 
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**[[2wxt]], [[1ca1]] - CpAT + Cd + Zn – ''Clostridium perfringens''<br />
 
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**[[1qm6]], [[1gyg]], [[1kho]] - CpAT + Zn <br />
 
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**[[2wy6]], [[2wxu]] – CpAT (mutant) + Ca + Cd + Zn<br />
 
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**[[1qmd]] - CpAT + Ca + Zn<br />
 
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**[[1olp]] - AT + Ca + Zn – ''Clostridium absonum''<br />
 
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**[[2vk9]] - AT – ''Clostridium novyi''<br />
 
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}}
 
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

α-hemolysin heptamer (PDB code 7ahl).

Drag the structure with the mouse to rotate

References

  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. ↑ Song L, Hobaugh MR, Shustak C, Cheley S, Bayley H, Gouaux JE. Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore. Science. 1996 Dec 13;274(5294):1859-66. PMID:8943190
  3. ↑ Verdon J, Girardin N, Lacombe C, Berjeaud JM, Héchard Y. delta-hemolysin, an update on a membrane-interacting peptide. Peptides. 2009 Apr;30(4):817-23. PMID:19150639 doi:10.1016/j.peptides.2008.12.017
  4. ↑ 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?)

Michal Harel, Mark Hoelzer, Wayne Decatur, Alexander Berchansky

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