Sandbox WWC6: Difference between revisions

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== Function ==
== Function ==
'''Alpha-hemolysin''' [https://en.wikipedia.org/wiki/Hemolysin#.CE.B1-hemolysin]  is a toxin secreted by Staphylococcus aureus as a pore-forming heptamer that binds to eukaryotic cell membranes.  This protein belongs to a family of beta-barrel pore-forming exotoxins[http://www.uniprot.org/uniprot/P09616].
'''Alpha-hemolysin''' [https://en.wikipedia.org/wiki/Hemolysin#.CE.B1-hemolysin]  is a toxin secreted by Staphylococcus aureus as a pore-forming heptamer that binds to eukaryotic cell membranes.  This protein belongs to a family of bacterial exotoxins[http://www.uniprot.org/uniprot/P09616]. The primary function of alpha-hemolysin is cytolytic, and is achieved by the release of cytosolic K<sup>+</sup> ions from the  through the hydrophilic, transmembrane portion of the beta-barrel pore[http://www.sciencedirect.com/science/article/pii/S0041010101001532].


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Revision as of 17:48, 15 April 2016

Function

Alpha-hemolysin [1] is a toxin secreted by Staphylococcus aureus as a pore-forming heptamer that binds to eukaryotic cell membranes. This protein belongs to a family of bacterial exotoxins[2]. The primary function of alpha-hemolysin is cytolytic, and is achieved by the release of cytosolic K+ ions from the through the hydrophilic, transmembrane portion of the beta-barrel pore[3].

1pgb

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N to C Sequence


 Amino Terminus                 Carboxy Terminus 


Let us color the two main forms of regular Secondary Structure in this protein. Alpha Helices appears in red,  Beta Strands  in yellow.


How many alpha helices are in this structure?

None.
One.
Four.


Tacrine within 1acj