1pvl
From Proteopedia
|
STRUCTURE OF THE PANTON-VALENTINE LEUCOCIDIN F COMPONENT FROM STAPHYLOCOCCUS AUREUS
Overview
BACKGROUND: Leucocidins and gamma-hemolysins are bi-component toxins, secreted by Staphylococcus aureus. These toxins activate responses of, specific cells and form lethal transmembrane pores. Their leucotoxic and, hemolytic activities involve the sequential binding and the synergistic, association of a class S and a class F component, which form, hetero-oligomeric complexes. The components of each protein class are, produced as non-associated, water-soluble proteins that undergo, conformational changes and oligomerization after recognition of their cell, targets. RESULTS: The crystal structure of the monomeric water-soluble, form of the F component of Panton-Valentine leucocidin (LukF-PV) has been, solved by the multiwavelength anomalous dispersion (MAD) method and, refined at 2.0 A resolution. The core of this three-domain protein is, similar to that of alpha-hemolysin, but significant differences occur in, regions that may be involved in the mechanism of pore formation. The, glycine-rich stem, which undergoes a major rearrangement in this process, forms an additional domain in LukF-PV. The fold of this domain is similar, to that of the neurotoxins and cardiotoxins from snake venom. CONCLUSIONS:, The structure analysis and a multiple sequence alignment of all toxic, components, suggest that LukF-PV represents the fold of any water-soluble, secreted protein in this family of transmembrane pore-forming toxins. The, comparison of the structures of LukF-PV and alpha-hemolysin provides some, insights into the mechanism of transmembrane pore formation for the, bi-component toxins, which may diverge from that of the alpha-hemolysin, heptamer.
About this Structure
1PVL is a Single protein structure of sequence from Staphylococcus aureus with MES as ligand. Full crystallographic information is available from OCA.
Reference
The structure of a Staphylococcus aureus leucocidin component (LukF-PV) reveals the fold of the water-soluble species of a family of transmembrane pore-forming toxins., Pedelacq JD, Maveyraud L, Prevost G, Baba-Moussa L, Gonzalez A, Courcelle E, Shepard W, Monteil H, Samama JP, Mourey L, Structure. 1999 Mar 15;7(3):277-87. PMID:10368297
Page seeded by OCA on Sun Nov 25 03:04:53 2007
