5AOF

Crystal structure of pneumolysin deletion mutant Delta146_147.

5AOF の概要

• エントリーDOI: 10.2210/pdb5aof/pdb
• 関連するPDBエントリー: 5AOD 5AOE
• 分子名称: PNEUMOLYSIN (2 entities in total)
• 機能のキーワード: toxin, cholesterol dependent cytolysin, pore forming toxin
• 由来する生物種: STREPTOCOCCUS PNEUMONIAE
• 細胞内の位置: Secreted : Q04IN8
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 54708.05

構造登録者

van Pee, K.,Yildiz, O. (登録日: 2015-09-10, 公開日: 2016-10-05, 最終更新日: 2024-01-10)

主引用文献

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

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: 28323617
DOI: 10.7554/eLife.23644

実験手法

X-RAY DIFFRACTION (2.45 Å)