2QK7
A covalent S-F heterodimer of staphylococcal gamma-hemolysin
Summary for 2QK7
| Entry DOI | 10.2210/pdb2qk7/pdb |
| Related | 1LKF 1PVL 1T5R 2LKF 3LKF |
| Descriptor | Gamma-hemolysin component A, Gamma-hemolysin component B (3 entities in total) |
| Functional Keywords | pore-forming toxin, beta-barrel, protein-protein interaction, molecular plasticity, covalent complex, cytolysis, hemolysis, secreted, toxin |
| Biological source | Staphylococcus aureus subsp. aureus More |
| Cellular location | Secreted: P0A074 |
| Total number of polymer chains | 2 |
| Total formula weight | 67606.41 |
| Authors | Roblin, P.,Guillet, V.,Maveyraud, L.,Mourey, L. (deposition date: 2007-07-10, release date: 2008-02-19, Last modification date: 2024-10-30) |
| Primary citation | Roblin, P.,Guillet, V.,Joubert, O.,Keller, D.,Erard, M.,Maveyraud, L.,Prevost, G.,Mourey, L. A covalent S-F heterodimer of leucotoxin reveals molecular plasticity of beta-barrel pore-forming toxins. Proteins, 71:485-496, 2008 Cited by PubMed Abstract: 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. PubMed: 18214982DOI: 10.1002/prot.21900 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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