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Hemolysin

From Proteopedia

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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>.
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</StructureSection>
 
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== 3D Structures of hemolysin ==
 
==3D Printed Physical Model of Hemolysin==
==3D Printed Physical Model of Hemolysin==
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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].
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].
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== 3D Structures of hemolysin ==
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[[Hemolysin 3D structures]]
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</StructureSection>
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== 3D Structures of hemolysin ==
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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**[[3o44]] – VcHL residues 161-741 – ''Vibrio cholerae''<br />
**[[3o44]] – VcHL residues 161-741 – ''Vibrio cholerae''<br />
**[[1xez]] – VcHL (mutant)<br />
**[[1xez]] – VcHL (mutant)<br />
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**[[6jkz]], [[6jl0]] - VvHL – ''Vibrio vulnificus''<br />
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**[[6jl1]], [[6jl2]] - VvHL (mutant)<br />
**[[3a57]] – HL 2 – ''Vibrio parahaemolyticus''<br />
**[[3a57]] – HL 2 – ''Vibrio parahaemolyticus''<br />
**[[3hvn]] – HL (mutant) – ''Streptococcus suis''<br />
**[[3hvn]] – HL (mutant) – ''Streptococcus suis''<br />
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**[[1mt0]] – EcHL B ATP-binding domain – ''Escherichia coli''<br />
**[[1mt0]] – EcHL B ATP-binding domain – ''Escherichia coli''<br />
**[[5c21]], [[5c22]] - EcHL D residues 57-333 <br />
**[[5c21]], [[5c22]] - EcHL D residues 57-333 <br />
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** [[6mru]], [[6mrw]], [[6mrt]] – EcHL E – Cryo EM<br />
**[[2wcd]] – EcHL E residues 2-303 – ''Escherichia coli''<br />
**[[2wcd]] – EcHL E residues 2-303 – ''Escherichia coli''<br />
**[[1qoy]], [[4pho]], [[4phq]] - EcHL E (mutant)<br />
**[[1qoy]], [[4pho]], [[4phq]] - EcHL E (mutant)<br />
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**[[2r2z]] – HL residues 346-435 – ''Enterococcus faecalis''<br />
**[[2r2z]] – HL residues 346-435 – ''Enterococcus faecalis''<br />
**[[4wx3]], [[4wx5]] - HL – ''Grimontia hollisae''<br />
**[[4wx3]], [[4wx5]] - HL – ''Grimontia hollisae''<br />
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**[[6d53]], [[6d5z]] - HL C-terminal – ''Bacillus cereus'' - NMR<br />
*Alpha-toxin
*Alpha-toxin

Revision as of 07:25, 25 July 2019

α-hemolysin heptamer (PDB code 7ahl).

Drag the structure with the mouse to rotate

3D Structures of hemolysin

Updated on 25-July-2019

A full page in Proteopedia exploring 7ahl is found here.

References

  1. ↑ 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
  2. ↑ Nizet V. Streptococcal beta-hemolysins: genetics and role in disease pathogenesis. Trends Microbiol. 2002 Dec;10(12):575-80. PMID:12564994

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Mark Hoelzer, Wayne Decatur, Alexander Berchansky

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