Skip to Main content Skip to Navigation
Journal articles

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

Abstract : 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.
Document type :
Journal articles
Complete list of metadatas

Cited literature [30 references]  Display  Hide  Download

https://hal-cnrs.archives-ouvertes.fr/hal-03004342
Contributor : Lionel Mourey <>
Submitted on : Friday, November 20, 2020 - 3:58:48 PM
Last modification on : Saturday, November 21, 2020 - 3:29:28 AM

File

pedelacq-intjmedmicrobiol00.pd...
Publisher files allowed on an open archive

Identifiers

  • HAL Id : hal-03004342, version 1

Collections

Citation

Jean-Denis Pedelacq, Gilles Prevost, Henri Monteil, Lionel Mourey, Jean-Pierre Samama. Crystal structure of the F component of the Panton-Valentine leucocidin. Journal of Medical Microbiology, Society for General Microbiology, 2000, 290, pp.395 - 401. ⟨hal-03004342⟩

Share

Metrics

Record views

2

Files downloads

6