20-21 November 2014
National Centre for Synchrotron Science
Australia/Melbourne timezone
Save the date: User Meeting 2015 - 26-27 November

Structural Studies of Streptolysin O from Streptococcus pyogenes

20 Nov 2014, 17:30
1h 30m
NCSS Exhibition Area ()

NCSS Exhibition Area

Australian Synchrotron 800 Blackburn Road Clayton VIC 3168
Board: 1005


Dr Susanne Feil (svi)


Cholesterol-dependent cytolysins (CDCs) constitute a family of bacterial toxins that form pores in many cell types. CDCs are secreted as water-soluble monomers, bind to cholesterol-rich membranes, oligomerise and insert into cell membranes. The presence of membrane cholesterol is required for the formation of large pores in cell membranes. In order to convert from a soluble monomeric protein into a membrane pore conformational changes of the three-dimensional structures of these toxins have to occur. Here, we present the three-dimensional structure of streptolysin O (SLO) from Streptococcus pyogenes. Comparison with other CDCs structures shows that the overall fold is similar but the C-terminal domain exhibits a different orientation with respect to the rest of the molecule. Additionally, the highly conserved region called the undecapeptide motif, which is involved in membrane recognition, adopts a different conformation in SLO compared to perfringolysin O (PFO), although the sequences in this region between the two toxins are identical.
Keywords or phrases (comma separated) bacterial toxins, cholesterol dependent cytolysin

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