Crystal structure of the F component of the Panton-Valentine leucocidin

Leucocidins and gamma -hemolysins are bi-component staphylococcal toxins th at form lytic transmembrane pores. Their cytotoxic activities involve the s ynergistic association of a class S and a class F component, produced as wa ter-soluble monomers which assemble on the surface of specific cells. The s tructure of the F protein from Panton-Valentine leucocidin, solved at 2.0 A ngstrom resolution, and sequence alignment suggest that it represents the f old of any secreted protein in this family of toxins. The comparison of thi s structure to that of the homoheptameric alpha -hemolysin provides some in sights into the molecular events that may occur during pore formation.