9fnq
From Proteopedia
Aerolysin double mutant K238A/K244A in styrene-maleic acid lipid particles
Structural highlights
FunctionAERA_AERHY Aerolysin is a cytolytic toxin exported by the Gram negative Aeromonas bacteria. The mature toxin binds to eukaryotic cells and aggregates to form holes approximately 3 nm in diameter, leading to destruction of the membrane permeability barrier and osmotic lysis. Publication Abstract from PubMedAerolysin is a beta-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 beta-barrel and its anchoring beta-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. Aerolysin Nanopore Structures Revealed at High Resolution in a Lipid Environment.,Anton JS, Iacovache I, Bada Juarez JF, Abriata LA, Perrin LW, Cao C, Marcaida MJ, Zuber B, Dal Peraro M J Am Chem Soc. 2025 Feb 3. doi: 10.1021/jacs.4c14288. PMID:39900531[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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