5AOF
Crystal structure of pneumolysin deletion mutant Delta146_147.
Summary for 5AOF
| Entry DOI | 10.2210/pdb5aof/pdb |
| Related | 5AOD 5AOE |
| Descriptor | PNEUMOLYSIN (2 entities in total) |
| Functional Keywords | toxin, cholesterol dependent cytolysin, pore forming toxin |
| Biological source | STREPTOCOCCUS PNEUMONIAE |
| Cellular location | Secreted : Q04IN8 |
| Total number of polymer chains | 1 |
| Total formula weight | 54708.05 |
| Authors | van Pee, K.,Yildiz, O. (deposition date: 2015-09-10, release date: 2016-10-05, Last modification date: 2024-01-10) |
| Primary citation | van Pee, K.,Neuhaus, A.,D'Imprima, E.,Mills, D.J.,Kuhlbrandt, W.,Yildiz, O. CryoEM structures of membrane pore and prepore complex reveal cytolytic mechanism of Pneumolysin. Elife, 6:-, 2017 Cited by PubMed Abstract: Many pathogenic bacteria produce pore-forming toxins to attack and kill human cells. We have determined the 4.5 Å structure of the ~2.2 MDa pore complex of pneumolysin, the main virulence factor of , by cryoEM. The pneumolysin pore is a 400 Å ring of 42 membrane-inserted monomers. Domain 3 of the soluble toxin refolds into two ~85 Å β-hairpins that traverse the lipid bilayer and assemble into a 168-strand β-barrel. The pore complex is stabilized by salt bridges between β-hairpins of adjacent subunits and an internal α-barrel. The apolar outer barrel surface with large sidechains is immersed in the lipid bilayer, while the inner barrel surface is highly charged. Comparison of the cryoEM pore complex to the prepore structure obtained by electron cryo-tomography and the x-ray structure of the soluble form reveals the detailed mechanisms by which the toxin monomers insert into the lipid bilayer to perforate the target membrane. PubMed: 28323617DOI: 10.7554/eLife.23644 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.45 Å) |
Structure validation
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