title: Crystal structure of the F component of the Panton-Valentine leucocidin.
abstract: Leucocidins and gamma-hemolysins are bi-component staphylococcal toxins that form lytic transmembrane pores. Their cytotoxic activities involve the synergistic association of a class S and a class F component, produced as water-soluble monomers which assemble on the surface of specific cells. The structure of the F protein from Panton-Valentine leucocidin, solved at 2.0 A resolution, and sequence alignment suggest that it represents the fold of any secreted protein in this family of toxins. The comparison of this structure to that of the homoheptameric alpha-hemolysin provides some insights into the molecular events that may occur during pore formation.
authors: Groupe de Cristallographie Biologique, Institut de Pharmacologie et de Biologie Structurale du CNRS, Toulouse, France.
authors: J D
authors: JD
authors: Pédelacq
authors: G
authors: G
authors: Prévost
authors: H
authors: H
authors: Monteil
authors: L
authors: L
authors: Mourey
authors: J P
authors: JP
authors: Samama
mesh_terms: D001427:Bacterial Toxins; D003460:Crystallization; D005098:Exotoxins / Q000737:chemistry*; D007956:Leukocidins / Q000737:chemistry*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D013211:Staphylococcus aureus
chemical_list: D001427:Bacterial Toxins; D005098:Exotoxins; D007956:Leukocidins; C078284:Panton-Valentine leukocidin