Hemolysin
From Proteopedia
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| - | + | <StructureSection load='7ahl' size='350' side='right' caption='α-hemolysin heptamer (PDB code [[7ahl]]).' scene=''>  | |
| + | == Function ==  | ||
| + | '''Hemolysin''' (HL) is exotoxin from bacteria which causes lysis of red blood cells<ref>PMID:20110774</ref>.   | ||
| + | *'''alpha-hemolysin''' is a transmembrane pore-forming heptameric molecule<ref>PMID:8943190</ref>.  See details for in [[Pore forming toxin, α-hemolysin]].    | ||
| + | *'''delta-hemolysin''' is a 26 amino acid peptide from the bacterium ''Staphylococcus'' exhibiting antimicrobial activity against'' Legionerlla'' <ref>PMID:19150639</ref>.   | ||
| - | '''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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| - | 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]].  | ||
For toxins in Proteopdia see [[Toxins]].  | For toxins in Proteopdia see [[Toxins]].  | ||
| - | ==   | + | == Relevance ==  | 
| + | HL acts as a virulence factor in the pathogenesis of invasive infections<ref>PMID:12564994</ref>.  | ||
| - | + | ==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.   | |
| - | + | [[Image:hemolysin1_centerForBioMolecularModeling.jpg|550px]]  | |
| - | + | [[Image:hemolysin2_centerForBioMolecularModeling.jpg|550px]]  | |
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| - | + | ====The MSOE Center for BioMolecular Modeling====  | |
| - | + | [[Image:CbmUniversityLogo.jpg | left | 150px]]  | |
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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].  | |
| - | + | == 3D Structures of hemolysin ==  | |
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| - | + | [[Hemolysin 3D structures]]  | |
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| - | + | </StructureSection>  | |
| - | **[[2wxt]], [[1ca1]] - CpAT + Cd + Zn – ''Clostridium perfringens''<br />  | ||
| - | **[[1qm6]], [[1gyg]], [[1kho]] - CpAT + Zn  <br />  | ||
| - | **[[2wy6]], [[2wxu]] – CpAT (mutant) + Ca + Cd + Zn<br />  | ||
| - | **[[1qmd]] - CpAT + Ca + Zn<br />  | ||
| - | **[[1olp]] - AT + Ca + Zn – ''Clostridium absonum''<br />  | ||
| - | **[[2vk9]] - AT – ''Clostridium novyi''<br />  | ||
| - | }}  | ||
== References ==  | == References ==  | ||
<references/>  | <references/>  | ||
[[Category:Topic Page]]  | [[Category:Topic Page]]  | ||
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References
- ↑ 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
 - ↑ 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
 - ↑ 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
 - ↑ Nizet V. Streptococcal beta-hemolysins: genetics and role in disease pathogenesis. Trends Microbiol. 2002 Dec;10(12):575-80. PMID:12564994
 
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