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Hemolysin
From Proteopedia
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== 3D Structures of hemolysin == | == 3D Structures of hemolysin == | ||
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| + | ''Updated December 2011'' | ||
===α-hemolysin=== | ===α-hemolysin=== | ||
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[[2qk7]] – SaHL-γ (mutant)<br /> | [[2qk7]] – SaHL-γ (mutant)<br /> | ||
| + | [[3b07]] - SaHL-γ | ||
===δ-hemolysin=== | ===δ-hemolysin=== | ||
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[[2wcd]] – EcHL E residues 2-303 – ''Escherichia coli''<br /> | [[2wcd]] – EcHL E residues 2-303 – ''Escherichia coli''<br /> | ||
[[1qoy]] - EcHL E (mutant)<br /> | [[1qoy]] - EcHL E (mutant)<br /> | ||
| - | [[1mt0]] – EcHL B ATP-binding domain | + | [[1mt0]] – EcHL B ATP-binding domain<br /> |
| + | [[2oai]], [[2r8d]] – HL corc_hlyc domain – ''Xylella fastidiosa''<br /> | ||
| + | [[2r2z]] – HL residues 346-435 – ''Enterococcus faecalis'' | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 07:14, 1 December 2011
Hemolysin (HL) is exotoxin from bacteria which causes lysis of red blood cells. See details for α-hemolysin in Pore forming toxin, α-hemolysin.
Contents |
3D Structures of hemolysin
Updated December 2011
α-hemolysin
3anz, 7ahl – SaHL-α – Staphylococcus aureus
3m2l, 3m4d - SaHL-α (mutant)
3m3r, 3m4e - SaHL-α (mutant) + β-cyclodextrin
β-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-hemolysin
2qk7 – SaHL-γ (mutant)
3b07 - SaHL-γ
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 - 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?)
Michal Harel, Mark Hoelzer, Wayne Decatur, Alexander Berchansky
