9FM6

Aerolysin Wildtype in styrene-maleic acid lipid particles

This is a non-PDB format compatible entry.

Summary for 9FM6

• Entry DOI: 10.2210/pdb9fm6/pdb
• Related: 5JZT
• EMDB information: 50549
• Descriptor: Aerolysin (1 entity in total)
• Functional Keywords: pore forming toxin styrene maleic acid lipid particle, toxin
• Biological source: Aeromonas hydrophila
• Total number of polymer chains: 7
• Total formula weight: 330296.06

Authors

Anton, J.S.,Bada Juarez, J.F.,Marcaida, M.J.,Dal Peraro, M. (deposition date: 2024-06-05, release date: 2025-02-12, Last modification date: 2025-07-02)

Primary citation

Anton, J.S.,Iacovache, I.,Bada Juarez, J.F.,Abriata, L.A.,Perrin, L.W.,Cao, C.,Marcaida, M.J.,Zuber, B.,Dal Peraro, M.
Aerolysin Nanopore Structures Revealed at High Resolution in a Lipid Environment.
J.Am.Chem.Soc., 147:4984-4992, 2025

PubMed Abstract: Aerolysin is a β-pore-forming toxin produced by most Aeromonas bacteria, which has attracted large attention in the field of nanopore sensing due to its narrow and charged pore lumen. Structurally similar proteins, belonging to the aerolysin-like family, are present throughout all kingdoms of life, but very few of them have been structurally characterized in a lipid environment. Here, we present the first high-resolution atomic cryo-EM structures of aerolysin prepore and pore in a membrane-like environment. These structures allow the identification of key interactions, which are relevant for understanding the pore formation mechanism and for correctly positioning the pore β-barrel and its anchoring β-turn motif in the membrane. Moreover, we elucidate at high resolution the architecture of key pore mutations and precisely identify four constriction rings in the pore lumen that are highly relevant for nanopore sensing experiments.

PubMed: 39900531
DOI: 10.1021/jacs.4c14288

Experimental method

ELECTRON MICROSCOPY (2.2 Å)