2BK2

The prepore structure of pneumolysin, obtained by fitting the alpha carbon trace of perfringolysin O into a cryo-EM map

Summary for 2BK2

• Entry DOI: 10.2210/pdb2bk2/pdb
• Related: 1M3I 1M3J 1PFO 2BK1
• EMDB information: 1106
• Descriptor: PERFRINGOLYSIN O (1 entity in total)
• Functional Keywords: cytolysis, hemolysis, thiol-activated cytolysin, toxin, cryoem, cytolytic protein
• Biological source: CLOSTRIDIUM PERFRINGENS
• Cellular location: Secreted: P19995
• Total number of polymer chains: 1
• Total formula weight: 50992.81

Authors

Tilley, S.J.,Orlova, E.V.,Gilbert, R.J.C.,Andrew, P.W.,Saibil, H.R. (deposition date: 2005-02-10, release date: 2005-05-04, Last modification date: 2024-05-08)

Primary citation

Tilley, S.J.,Orlova, E.V.,Gilbert, R.J.C.,Andrew, P.W.,Saibil, H.R.
Structural Basis of Pore Formation by the Bacterial Toxin Pneumolysin
Cell(Cambridge,Mass.), 121:247-, 2005

PubMed Abstract: The bacterial toxin pneumolysin is released as a soluble monomer that kills target cells by assembling into large oligomeric rings and forming pores in cholesterol-containing membranes. Using cryo-EM and image processing, we have determined the structures of membrane-surface bound (prepore) and inserted-pore oligomer forms, providing a direct observation of the conformational transition into the pore form of a cholesterol-dependent cytolysin. In the pore structure, the domains of the monomer separate and double over into an arch, forming a wall sealing the bilayer around the pore. This transformation is accomplished by substantial refolding of two of the four protein domains along with deformation of the membrane. Extension of protein density into the bilayer supports earlier predictions that the protein inserts beta hairpins into the membrane. With an oligomer size of up to 44 subunits in the pore, this assembly creates a transmembrane channel 260 A in diameter lined by 176 beta strands.

PubMed: 15851031
DOI: 10.1016/J.CELL.2005.02.033

Experimental method

ELECTRON MICROSCOPY (28 Å)