Hemolysin

From Proteopedia

(Difference between revisions)

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 </StructureSection>
-== 3D Structures of hemolysin ==
-Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
-{{#tree:id=OrganizedByTopic|openlevels=0|
-*α-hemolysin
-**[[3anz]], [[7ahl]] – SaHL-α – ''Staphylococcus aureus''<br />
-A full page in Proteopedia exploring [[7ahl]] is found [[Pore_forming_toxin,_α-hemolsyin|here]].<br/>
-**[[3m2l]], [[3m4d]], [[4p24]], [[4yhd]] - SaHL-α (mutant)<br />
-**[[3m3r]], [[3m4e]] - SaHL-α (mutant) + β-cyclodextrin<br />
-**[[4idj]], [[4u6v]] - SaHL-α + antibody<br />
-*β-hemolysin
-**[[3k55]] – SaHL-β)<br />
-**[[3i5v]] - SaHL-β residues 35-330)<br />
-**[[3i41]] - SaHL-β residues 35-330 (mutant)<br />
-**[[3i46]], [[3i48]] - SaHL-β residues 35-330 (mutant)<br /> + metal ion
-*γ-hemolysin
-**[[2qk7]] – SaHL-γ component A (mutant) +B (mutant)<br />
-**[[3b07]] - SaHL-γ component A+B<br />
-**[[4p1x]] - SaHL-γ component B (mutant)+C<br />
-**[[4p1y]] - SaHL-γ component A + B (mutant)<br />
-*δ-hemolysin
-**[[2kam]] – SaHL-δ - NMR
-*Hemolysin
-**[[3o44]] – VcHL residues 161-741 – ''Vibrio cholerae''<br />
-**[[1xez]] – VcHL (mutant)<br />
-**[[6jkz]], [[6jl0]] - VvHL – ''Vibrio vulnificus''<br />
-**[[6jl1]], [[6jl2]] - VvHL (mutant)<br />
-**[[3a57]] – HL 2 – ''Vibrio parahaemolyticus''<br />
-**[[3hvn]] – HL (mutant) – ''Streptococcus suis''<br />
-**[[3fy3]], [[5keh]], [[5kf3]], [[4w8q]], [[5kdk]] – PmHL A residues 30-265 – ''Proteus mirabilis''<br />
-**[[5sz8]], [[5kkd]], [[4w8r]], [[4w8s]], [[4w8t]] - PmHL A residues 30-234 (mutant)<br />
-**[[1mt0]] – EcHL B ATP-binding domain – ''Escherichia coli''<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 />
-**[[1qoy]], [[4pho]], [[4phq]] - EcHL E (mutant)<br />
-**[[2oai]], [[2r8d]] – HL corc_hlyc domain – ''Xylella fastidiosa''<br />
-**[[2r2z]] – HL residues 346-435 – ''Enterococcus faecalis''<br />
-**[[4wx3]], [[4wx5]] - HL – ''Grimontia hollisae''<br />
-**[[6d53]], [[6d5z]] - HL C-terminal – ''Bacillus cereus'' - NMR<br />
-*Alpha-toxin
-**[[2wxt]], [[1ca1]] - CpAT + Cd + Zn – ''Clostridium perfringens''<br />
-**[[1qm6]], [[1gyg]], [[1kho]] - CpAT + Zn  <br />
-**[[2wy6]], [[2wxu]] – CpAT (mutant) + Ca + Cd + Zn<br />
-**[[1qmd]] - CpAT + Ca + Zn<br />
-**[[1olp]] - AT + Ca + Zn – ''Clostridium absonum''<br />
-**[[2vk9]] - AT – ''Clostridium novyi''<br />
-}}
 == References ==
 <references/>
 [[Category:Topic Page]]

Revision as of 07:27, 25 July 2019

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α-hemolysin heptamer (PDB code 7ahl).

Show:Asymmetric Unit Biological Assembly

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1 Function
2 Relevance
3 3D Printed Physical Model of Hemolysin
- 3.1 The MSOE Center for BioMolecular Modeling
4 3D Structures of hemolysin

Function

Hemolysin (HL) is exotoxin from bacteria which causes lysis of red blood cells^[1]. 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.

See details for α-hemolysin in Pore forming toxin, α-hemolysin.

See details of hemolysin E in Molecular Playground/ClyA.

For toxins in Proteopdia see Toxins.

Relevance

HL acts as a virulence factor in the pathogenesis of invasive infections^[2].

3D Printed Physical Model of Hemolysin

Shown below is a 3D printed physical model of Hemolysin. The model is shown in alpha carbon backbone format with each chain colored uniquely.

The MSOE Center for BioMolecular Modeling

The 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 Model Gallery.

3D Structures of hemolysin

Hemolysin 3D structures

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