Structural studies of Streptococcus pyogenes streptolysin O provide insights into the early steps of membrane penetration.

ABSTRACT: Cholesterol-dependent cytolysins (CDCs) are a large family of bacterial toxins that exhibit a dependence on the presence of membrane cholesterol in forming large pores in cell membranes. Significant changes in the three-dimensional structure of these toxins are necessary to convert the soluble monomeric protein into a membrane pore. We have determined the crystal structure of the archetypical member of the CDC family, streptolysin O (SLO), a virulence factor from Streptococcus pyogenes. The overall fold is similar to previously reported CDC structures, although the C-terminal domain is in a different orientation with respect to the rest of the molecule. Surprisingly, a signature stretch of CDC sequence called the undecapeptide motif, a key region involved in membrane recognition, adopts a

SUBMITTER: Feil SC 

PROVIDER: S-EPMC4323271 | biostudies-literature | 2014 Feb

REPOSITORIES: biostudies-literature