Sandbox WWC6: Difference between revisions

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== Function ==
== Function ==
'''Alpha-hemolysin''' [https://en.wikipedia.org/wiki/Hemolysin#.CE.B1-hemolysin]  is secreted by Staphylococcus aureus as a pore-forming toxin that binds to Eukaryotic cell membranes, and
'''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].
 


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<applet load='1pgb' size='350' frame='true' align='right' caption='1pgb' scene='Insert optional scene name here' />

Revision as of 17:35, 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 beta-barrel pore-forming exotoxins[2].

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