Hemolysin

Template:STRUCTURE 3k55

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.

3D Structures of hemolysin3D Structures of hemolysin

Updated December 2011

α-hemolysinα-hemolysin

3anz, 7ahl – SaHL-α – Staphylococcus aureus
A full page devoted to exploring 7ahl is found here Pore_forming_toxin,_α-hemolsyin.
3m2l, 3m4d - SaHL-α (mutant)
3m3r, 3m4e - SaHL-α (mutant) + β-cyclodextrin

β-hemolysinβ-hemolysin

3k55 – SaHL-β)
3i5v - SaHL-β residues 35-330)
3i41 - SaHL-β residues 35-330 (mutant)
3i46, 3i48 - SaHL-β residues 35-330 (mutant)
+ metal ion

γ-hemolysinγ-hemolysin

2qk7 – SaHL-γ (mutant)
3b07 - SaHL-γ

δ-hemolysinδ-hemolysin

2kam – SaHL-δ - NMR

HemolysinHemolysin

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 - EcHL E (mutant)
1mt0 – EcHL B ATP-binding domain
2oai, 2r8d – HL corc_hlyc domain – Xylella fastidiosa
2r2z – HL residues 346-435 – Enterococcus faecalis

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Wayne Decatur, Alexander Berchansky, Michal Harel, Mark Hoelzer