5LY6

CryoEM structure of the membrane pore complex of Pneumolysin at 4.5A

Summary for 5LY6

• Entry DOI: 10.2210/pdb5ly6/pdb
• EMDB information: 4118
• Descriptor: Pneumolysin (1 entity in total)
• Functional Keywords: bacterial toxins, pore complex, cryoem structure, cholesterol-dependent cytolysin, pneumolysin, membrane pore, toxin
• Biological source: Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466)
• Total number of polymer chains: 1
• Total formula weight: 52866.07

Authors

van Pee, K.,Neuhaus, A.,D'Imprima, E.,Mills, D.J.,Kuehlbrandt, W.,Yildiz, O. (deposition date: 2016-09-24, release date: 2017-04-05, Last modification date: 2024-05-15)

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

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

Experimental method

ELECTRON MICROSCOPY (4.5 Å)