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SUMMARY:Structural Studies of Streptolysin O from Streptococcus pyogenes
DTSTART;VALUE=DATE-TIME:20141120T063000Z
DTEND;VALUE=DATE-TIME:20141120T080000Z
DTSTAMP;VALUE=DATE-TIME:20260305T180310Z
UID:indico-contribution-671@events01.synchrotron.org.au
DESCRIPTION:Speakers: Susanne Feil (svi)\nCholesterol-dependent cytolysins
  (CDCs) constitute a family of bacterial toxins that form pores in many ce
 ll types. CDCs are secreted as water-soluble monomers\, bind to cholestero
 l-rich membranes\, oligomerise and insert into cell membranes. The presenc
 e 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 st
 ructure of streptolysin O (SLO) from Streptococcus pyogenes. Comparison wi
 th 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 und
 ecapeptide motif\, which is involved in membrane recognition\, adopts a di
 fferent conformation in SLO compared to perfringolysin O (PFO)\, although 
 the sequences in this region between the two toxins are identical.\n\nhttp
 s://events01.synchrotron.org.au/event/3/contributions/671/
LOCATION: NCSS Exhibition Area
URL:https://events01.synchrotron.org.au/event/3/contributions/671/
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