4P1X
Crystal structure of staphylococcal LUK prepore
Summary for 4P1X
| Entry DOI | 10.2210/pdb4p1x/pdb |
| Related | 1luk 2luk 3b07 3luk 4P1Y 4P24 |
| Descriptor | Gamma-hemolysin component C, Gamma-hemolysin component B, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (4 entities in total) |
| Functional Keywords | pore forming toxin, toxin |
| Biological source | Staphylococcus aureus More |
| Total number of polymer chains | 8 |
| Total formula weight | 276979.04 |
| Authors | Yamashita, D.,Tanaka, Y.,Tanaka, I.,Yao, M. (deposition date: 2014-02-28, release date: 2014-10-01, Last modification date: 2023-12-27) |
| Primary citation | Yamashita, D.,Sugawara, T.,Takeshita, M.,Kaneko, J.,Kamio, Y.,Tanaka, I.,Tanaka, Y.,Yao, M. Molecular basis of transmembrane beta-barrel formation of staphylococcal pore-forming toxins. Nat Commun, 5:4897-4897, 2014 Cited by PubMed Abstract: Pathogenic bacteria secrete pore-forming toxins (PFTs) to attack target cells. PFTs are expressed as water-soluble monomeric proteins, which oligomerize into nonlytic prepore intermediates on the target cell membrane before forming membrane-spanning pores. Despite a wealth of biochemical data, the lack of high-resolution prepore structural information has hampered understanding of the β-barrel formation process. Here, we report crystal structures of staphylococcal γ-haemolysin and leucocidin prepores. The structures reveal a disordered bottom half of the β-barrel corresponding to the transmembrane region, and a rigid upper extramembrane half. Spectroscopic analysis of fluorescently labelled mutants confirmed that the prepore is distinct from the pore within the transmembrane region. Mutational analysis also indicates a pivotal role for the glycine residue located at the lipid-solvent interface as a 'joint' between the two halves of the β-barrel. These observations suggest a two-step transmembrane β-barrel pore formation mechanism in which the upper extramembrane and bottom transmembrane regions are formed independently. PubMed: 25263813DOI: 10.1038/ncomms5897 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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