%0 Journal Article %T Crystal structure of the F component of the Panton-Valentine leucocidin %+ Institut de pharmacologie et de biologie structurale (IPBS) %A Pedelacq, Jean-Denis %A Prevost, Gilles %A Monteil, Henri %A Mourey, Lionel %A Samama, Jean-Pierre %< avec comité de lecture %J J. Med. Microbial %V 290 %P 395 - 401 %8 2000 %D 2000 %Z Life Sciences [q-bio]Journal articles %X Leucocidins and y-hemolysins are bi-component staphylococcal toxins that form lytic transmem-brane 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 a-hemolysin provides some insights into the molecular events that may occur during pore formation. %G English %2 https://cnrs.hal.science/hal-03004342/document %2 https://cnrs.hal.science/hal-03004342/file/pedelacq-intjmedmicrobiol00.pdf %L hal-03004342 %U https://cnrs.hal.science/hal-03004342 %~ UNIV-TLSE3 %~ CNRS %~ IPBS %~ UNIV-UT3 %~ UT3-INP %~ UT3-TOULOUSEINP