Hemolysin

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{{STRUCTURE_3k55| PDB=3k55 | SIZE=400| SCENE= |right|CAPTION=β-hemolysin, [[3k55]] }}
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<StructureSection load='7ahl' size='350' side='right' caption='α-hemolysin heptamer (PDB code [[7ahl]]).' scene=''>
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== Function ==
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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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'''Hemolysin''' (HL) is exotoxin from bacteria which causes lysis of red blood cells. See details for α-hemolysin in [[Pore forming toxin, α-hemolysin]]. For toxins in Proteopdia see [[Toxins]].
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See details of hemolysin E in [[Molecular Playground/ClyA]].
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{{TOC limit|limit=2}}
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For toxins in Proteopdia see [[Toxins]].
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== 3D Structures of hemolysin ==
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== Relevance ==
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HL acts as a virulence factor in the pathogenesis of invasive infections<ref>PMID:12564994</ref>.
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''Updated December 2011''
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==3D Printed Physical Model of Hemolysin==
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===α-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.
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[[3anz]], [[7ahl]] – SaHL-α – S''taphylococcus aureus''<br />
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[[Image:hemolysin1_centerForBioMolecularModeling.jpg|550px]]
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A full page in Proteopedia exploring [[7ahl]] is found [[Pore_forming_toxin,_α-hemolsyin|here]].<br/>
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[[Image:hemolysin2_centerForBioMolecularModeling.jpg|550px]]
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[[3m2l]], [[3m4d]] - SaHL-α (mutant)<br />
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[[3m3r]], [[3m4e]] - SaHL-α (mutant) + β-cyclodextrin
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===β-hemolysin===
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====The MSOE Center for BioMolecular Modeling====
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[[3k55]] – SaHL-β)<br />
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[[Image:CbmUniversityLogo.jpg | left | 150px]]
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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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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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[[2qk7]] – SaHL-γ (mutant)<br />
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== 3D Structures of hemolysin ==
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[[3b07]] - SaHL-γ
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===δ-hemolysin===
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[[2kam]] – SaHL-δ - NMR
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===Hemolysin===
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[[Hemolysin 3D structures]]
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[[3o44]] – VcHL residues 161-741 – ''Vibrio cholerae''<br />
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</StructureSection>
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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]] – HL A residues 30-265 – ''Proteus mirabilis''<br />
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[[2wcd]] – EcHL E residues 2-303 – ''Escherichia coli''<br />
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[[1qoy]] - EcHL E (mutant)<br />
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[[1mt0]] – EcHL B ATP-binding domain<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''
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== References ==
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<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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