2BK2

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

2BK2 の概要

• エントリーDOI: 10.2210/pdb2bk2/pdb
• 関連するPDBエントリー: 1M3I 1M3J 1PFO 2BK1
• EMDBエントリー: 1106
• 分子名称: PERFRINGOLYSIN O (1 entity in total)
• 機能のキーワード: cytolysis, hemolysis, thiol-activated cytolysin, toxin, cryoem, cytolytic protein
• 由来する生物種: CLOSTRIDIUM PERFRINGENS
• 細胞内の位置: Secreted: P19995
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 50992.81

構造登録者

Tilley, S.J.,Orlova, E.V.,Gilbert, R.J.C.,Andrew, P.W.,Saibil, H.R. (登録日: 2005-02-10, 公開日: 2005-05-04, 最終更新日: 2024-05-08)

主引用文献

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

実験手法

ELECTRON MICROSCOPY (28 Å)