Sandbox WWC6: Difference between revisions

[[Hemolysins]] [https://en.wikipedia.org/wiki/Hemolysin#.CE.B1-hemolysin]  are a  lipid or protein toxins secreted by pathogens that lyse erythrocyte and some bacterial cell membranes.  These toxins belong to a family of microbial exotoxins called cytolysins, which act on a broad number of cells[http://www.uniprot.org/uniprot/P09616]. The primary function of peptide hemolysins is pore formation at the cell membranes creating acytolytic effect, and is achieved by the release of cytosolic ions and small molecules through the hydrophilic, transmembrane portion of the beta-barrel pore[http://www.sciencedirect.com/science/article/pii/S0041010101001532].

Hemolysins have three structural variations: alpha, beta, and gamma. These hemolysin types are comprised of di-, hepta- or octomeric subunits.

<scene name='69/696302/Alpha-hemolysin/1'>Alpha-hemolysin</scene>

[http://proteopedia.org/wiki/index.php/Pore_forming_toxin,_%CE%B1-hemolysin Alpha hemolysin] causes a partial lysis of red blood cells.  The heptameric pore assembles from water-soluble subunits.  The alpha subunit, depicted right, consists seven identical monomeric units that exhibit rotational symmetry in oligomerized form.  Each distinct subunit is differently colored for easy identification.  The beta-barrel transmembrane domain is 50 Å in length <ref>http://www.ks.uiuc.edu/Research/hemolysin/<ref>.

<scene name='69/696302/Beta-hemolysin/2'>Beta-hemolysin</scene>

Beta-hemolysins cause a total lysis of red blood cells.

<scene name='69/696302/Beta-hemolysin/1'>Gamma-hemolysin</scene>