5GAQ: Cryo-em Structure Of The Lysenin Pore

Lysenin from the coelomic fluid of the earthworm Eisenia fetida belongs to the aerolysin family of small beta-pore-forming toxins (beta-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 A resolution. The nonameric assembly reveals a long beta-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 beta-barrel of the channel.
PDB ID: 5GAQDownload
MMDB ID: 138166
PDB Deposition Date: 2016/1/5
Updated in MMDB: 2016/10
Experimental Method:
electron microscopy
Resolution: 3.14  Å
Source Organism:
Similar Structures:
Biological Unit for 5GAQ: nonameric; determined by author and by software (PISA)
Molecular Components in 5GAQ
Label Count Molecule
Proteins (9 molecules)
Molecule annotation
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