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-Structure paper
タイトル | CryoEM structures of membrane pore and prepore complex reveal cytolytic mechanism of Pneumolysin. |
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ジャーナル・号・ページ | Elife, Vol. 6, Year 2017 |
掲載日 | 2017年3月21日 |
著者 | Katharina van Pee / Alexander Neuhaus / Edoardo D'Imprima / Deryck J Mills / Werner Kühlbrandt / Özkan Yildiz / |
PubMed 要旨 | 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 ...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. |
リンク | Elife / PubMed:28323617 / PubMed Central |
手法 | EM (単粒子) / X線回折 |
解像度 | 2.45 - 4.5 Å |
構造データ | EMDB-4118, PDB-5ly6: PDB-5aoe: PDB-5aof: |
化合物 | ChemComp-HOH: |
由来 |
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キーワード | TOXIN / CHOLESTEROL DEPENDENT CYTOLYSIN / PORE FORMING TOXIN / Bacterial toxins / pore complex / cryoEM structure / cholesterol-dependent cytolysin / Pneumolysin / membrane pore |