Hemolysin: Difference between revisions
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<StructureSection load='7ahl' size='350' side='right' caption='α-hemolysin heptamer (PDB code [[7ahl]]).' scene=''> | |||
== Function == | == 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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== 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>. | ||
</StructureSection> | |||
== 3D Structures of hemolysin == | == 3D Structures of hemolysin == | ||
Revision as of 09:09, 7 February 2017
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3D Structures of hemolysin
Updated on 07-February-2017
A full page in Proteopedia exploring Toxins 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
References
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Mark Hoelzer, Wayne Decatur, Marius Mihasan, Alexander Berchansky