5GAQ

Cryo-EM structure of the Lysenin Pore

5GAQ の概要

• エントリーDOI: 10.2210/pdb5gaq/pdb
• EMDBエントリー: 8015
• 分子名称: Lysenin (1 entity in total)
• 機能のキーワード: pore forming protein, aerolysin, toxin
• 由来する生物種: Eisenia fetida (Red wiggler worm)
• タンパク質・核酸の鎖数: 9
• 化学式量合計: 314795.21

構造登録者

Savva, C.G.,Bokori-Brown, M.,Martin, T.G.,Titball, R.W.,Naylor, C.E.,Basak, A.K. (登録日: 2016-01-05, 公開日: 2016-04-06, 最終更新日: 2024-05-15)

主引用文献

Bokori-Brown, M.,Martin, T.G.,Naylor, C.E.,Basak, A.K.,Titball, R.W.,Savva, C.G.
Cryo-EM structure of lysenin pore elucidates membrane insertion by an aerolysin family protein
Nat Commun, 7:11293-11293, 2016

PubMed Abstract: Lysenin from the coelomic fluid of the earthworm Eisenia fetida belongs to the aerolysin family of small β-pore-forming toxins (β-PFTs), some members of which are pathogenic to humans and animals. Despite efforts, a high-resolution structure of a channel for this family of proteins has been elusive and therefore the mechanism of activation and membrane insertion remains unclear. Here we determine the pore structure of lysenin by single particle cryo-EM, to 3.1 Å resolution. The nonameric assembly reveals a long β-barrel channel spanning the length of the complex that, unexpectedly, includes the two pre-insertion strands flanking the hypothetical membrane-insertion loop. Examination of other members of the aerolysin family reveals high structural preservation in this region, indicating that the membrane-insertion pathway in this family is conserved. For some toxins, proteolytic activation and pro-peptide removal will facilitate unfolding of the pre-insertion strands, allowing them to form the β-barrel of the channel.

PubMed: 27048994
DOI: 10.1038/ncomms11293

実験手法

ELECTRON MICROSCOPY (3.1 Å)