The three-dimensional structure of trypsin-treated Staphylococcus aureus α-toxin

Trypsin treatment of staphylococcal α-toxin cleaves the molecule into two roughly equally sized parts, which ] results in inactivation of the toxin. Tetragonal arrays of oligomers, closely resembling the native ones, can however be formed on lipid layers. From tilted views of negatively stained crystals a 31) structure to 23 Å resolution has been determined by electron microscopy and image processing. On comparison with the 31) structure of the native ot-toxin (Olofsson et al., J. Mol. Biol. 214, 299–306, 1990) the subdomains are more separated, confirming the differences found when comparing the projection maps (Olofsson et al., J. Struct. Biol. 106, 199–204, 1991). The tryptic cleavage takes place in a postulated hinge region. The results are consistent with the hypothesis that the conformational change required for inducing the membrane permeabilizing property takes place in this region. Furthermore, we present a refined projection map at approximately 10 Å resolution based on the analysis of a large number of crystals using unbending methods.