5EC5

Crystal structure of lysenin pore

Summary for 5EC5

• Entry DOI: 10.2210/pdb5ec5/pdb
• Descriptor: Lysenin, MERCURIBENZOIC ACID, MERCURY (II) ION, ... (4 entities in total)
• Functional Keywords: invertebrate cytolysin, nonamer, functional pore, nanopore, toxin
• Biological source: Eisenia fetida (Red wiggler worm)
• Cellular location: Secreted : O18423
• Total number of polymer chains: 18
• Total formula weight: 611727.89

Authors

Podobnik, M.,Savory, P.,Rojko, N.,Kisovec, M.,Bruce, M.,Jayasinghe, L.,Anderluh, G. (deposition date: 2015-10-20, release date: 2016-05-18, Last modification date: 2024-05-08)

Primary citation

Podobnik, M.,Savory, P.,Rojko, N.,Kisovec, M.,Wood, N.,Hambley, R.,Pugh, J.,Wallace, E.J.,McNeill, L.,Bruce, M.,Liko, I.,Allison, T.M.,Mehmood, S.,Yilmaz, N.,Kobayashi, T.,Gilbert, R.J.,Robinson, C.V.,Jayasinghe, L.,Anderluh, G.
Crystal structure of an invertebrate cytolysin pore reveals unique properties and mechanism of assembly.
Nat Commun, 7:11598-11598, 2016

PubMed Abstract: The invertebrate cytolysin lysenin is a member of the aerolysin family of pore-forming toxins that includes many representatives from pathogenic bacteria. Here we report the crystal structure of the lysenin pore and provide insights into its assembly mechanism. The lysenin pore is assembled from nine monomers via dramatic reorganization of almost half of the monomeric subunit structure leading to a β-barrel pore ∼10 nm long and 1.6-2.5 nm wide. The lysenin pore is devoid of additional luminal compartments as commonly found in other toxin pores. Mutagenic analysis and atomic force microscopy imaging, together with these structural insights, suggest a mechanism for pore assembly for lysenin. These insights are relevant to the understanding of pore formation by other aerolysin-like pore-forming toxins, which often represent crucial virulence factors in bacteria.

PubMed: 27176125
DOI: 10.1038/ncomms11598

Experimental method

X-RAY DIFFRACTION (3.1 Å)