Structural highlights
2qk7 is a 2 chain structure with sequence from Staaw. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Related: | 1lkf, 2lkf, 3lkf, 1pvl, 1t5r |
| Gene: | hlgA, hlg2 (STAAW), hlgB (STAAW) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[HLGA_STAAU] Toxin that seems to act by forming pores in the membrane of the cell. Has a hemolytic and a leucotoxic activity. [HLGB_STAAU] Toxin that seems to act by forming pores in the membrane of the cell. Has a hemolytic and a leucotoxic activity.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ 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. 2008 Jan 23;71(1):485-496. PMID:18214982 doi:10.1002/prot.21900
