5GAQ
Cryo-EM structure of the Lysenin Pore
Summary for 5GAQ
| Entry DOI | 10.2210/pdb5gaq/pdb |
| EMDB information | 8015 |
| Descriptor | Lysenin (1 entity in total) |
| Functional Keywords | pore forming protein, aerolysin, toxin |
| Biological source | Eisenia fetida (Red wiggler worm) |
| Total number of polymer chains | 9 |
| Total formula weight | 314795.21 |
| Authors | Savva, C.G.,Bokori-Brown, M.,Martin, T.G.,Titball, R.W.,Naylor, C.E.,Basak, A.K. (deposition date: 2016-01-05, release date: 2016-04-06, Last modification date: 2024-05-15) |
| Primary citation | 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 Cited by 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: 27048994DOI: 10.1038/ncomms11293 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.1 Å) |
Structure validation
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