2qk7: Difference between revisions
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'''A covalent S-F heterodimer of staphylococcal gamma-hemolysin''' | '''A covalent S-F heterodimer of staphylococcal gamma-hemolysin''' | ||
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[[Category: Mourey, L.]] | [[Category: Mourey, L.]] | ||
[[Category: Roblin, P.]] | [[Category: Roblin, P.]] | ||
[[Category: | [[Category: Beta-barrel]] | ||
[[Category: | [[Category: Covalent complex]] | ||
[[Category: | [[Category: Cytolysis]] | ||
[[Category: | [[Category: Hemolysis]] | ||
[[Category: | [[Category: Molecular plasticity]] | ||
[[Category: | [[Category: Pore-forming toxin]] | ||
[[Category: | [[Category: Protein-protein interaction]] | ||
[[Category: | [[Category: Secreted]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 15:06:17 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 12:06, 4 May 2008
A covalent S-F heterodimer of staphylococcal gamma-hemolysin
Overview
Staphylococcal leucotoxins, leucocidins, and gamma-hemolysins are bicomponent beta-barrel pore-forming toxins (beta-PFTs). Their production is associated with several clinical diseases. They have cytotoxic activity due to the synergistic action of a class S component and a class F component, which are secreted as water-soluble monomers and form hetero-oligomeric transmembrane pores, causing the lysis of susceptible cells. Structural information is currently available for the monomeric S and F proteins and the homoheptamer formed by the related alpha-hemolysin. These structures illustrate the start and end points in the mechanistic framework of beta-PFT assembly. Only limited structural data exist for the intermediate stages, including hetero-oligomeric complexes of leucotoxins. We investigated the protein-protein interactions responsible for maintaining the final bipartite molecular architecture and describe here the high-resolution crystal structure and low-resolution solution structure of a site-specific cross-linked heterodimer of gamma-hemolysin (HlgA T28C-HlgB N156C), which were solved by X-ray crystallography and small angle X-ray scattering, respectively. These structures reveal a molecular plasticity of beta-PFTs, which may facilitate the transition from membrane-bound monomers to heterodimers. Proteins 2008. (c) 2008 Wiley-Liss, Inc.
About this Structure
2QK7 is a Protein complex structure of sequences from Staphylococcus aureus. Full crystallographic information is available from OCA.
Reference
A covalent S-F heterodimer of leucotoxin reveals molecular plasticity of beta-barrel pore-forming toxins., Roblin P, Guillet V, Joubert O, Keller D, Erard M, Maveyraud L, Prevost G, Mourey L, Proteins. 2008 Jan 23;71(1):485-496. PMID:18214982 Page seeded by OCA on Sun May 4 15:06:17 2008
