Hemolysin: Difference between revisions
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{{STRUCTURE_7ahl| PDB=7ahl | SIZE=400| SCENE= |right|CAPTION=α-hemolysin heptamer, [[7ahl]] }} | {{STRUCTURE_7ahl| PDB=7ahl | SIZE=400| SCENE= |right|CAPTION=α-hemolysin heptamer, [[7ahl]] }} | ||
== 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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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 Structures of hemolysin == | == 3D Structures of hemolysin == | ||
Revision as of 08:01, 21 March 2016
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].
3D Structures of hemolysin
Updated on 21-March-2016
A full page in Proteopedia exploring 7ahl is found here.
- β-hemolysin
- γ-hemolysin
- 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
- 3o44 – VcHL residues 161-741 – Vibrio cholerae
- Alpha-toxin
- ↑ 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
- ↑ Nizet V. Streptococcal beta-hemolysins: genetics and role in disease pathogenesis. Trends Microbiol. 2002 Dec;10(12):575-80. PMID:12564994
References
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Mark Hoelzer, Wayne Decatur, Marius Mihasan, Alexander Berchansky
