Hemolysin
From Proteopedia
(Difference between revisions)
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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 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]. | ||
| + | == 3D Structures of hemolysin == | ||
| + | [[Hemolysin 3D structures]] | ||
| + | </StructureSection> | ||
| + | == 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 /> | ||
| + | **[[6jkz]], [[6jl0]] - VvHL – ''Vibrio vulnificus''<br /> | ||
| + | **[[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 /> | ||
| + | ** [[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 /> | ||
| + | **[[6d53]], [[6d5z]] - HL C-terminal – ''Bacillus cereus'' - NMR<br /> | ||
*Alpha-toxin | *Alpha-toxin | ||
Revision as of 07:25, 25 July 2019
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3D Structures of hemolysin
Updated on 25-July-2019
A full page in Proteopedia exploring 7ahl is found here.
References
- ↑ 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
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