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TitleAerolysin Nanopore Structures Revealed at High Resolution in a Lipid Environment.
Journal, issue, pagesJ Am Chem Soc, Vol. 147, Issue 6, Page 4984-4992, Year 2025
Publish dateFeb 12, 2025
AuthorsJana S Anton / Ioan Iacovache / Juan F Bada Juarez / Luciano A Abriata / Louis W Perrin / Chan Cao / Maria J Marcaida / Benoît Zuber / Matteo Dal Peraro /
PubMed AbstractAerolysin 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 ...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.
External linksJ Am Chem Soc / PubMed:39900531 / PubMed Central
MethodsEM (single particle)
Resolution2.1 - 2.6 Å
Structure data

EMDB-50549, PDB-9fm6:
Aerolysin Wildtype in styrene-maleic acid lipid particles
Method: EM (single particle) / Resolution: 2.2 Å

EMDB-50562, PDB-9fml:
Aerolysin heptamer in membrane inserted form reconstituted in amphipoles.
Method: EM (single particle) / Resolution: 2.2 Å

EMDB-50576, PDB-9fmx:
Aerolysin Y221G - prepore
Method: EM (single particle) / Resolution: 2.2 Å

EMDB-50578: aerolysin WT pore in LMNG:CHS
Method: EM (single particle) / Resolution: 2.6 Å

EMDB-50601, PDB-9fnp:
Aerolysin mutant K238A in styrene-maleic acid lipid particles
Method: EM (single particle) / Resolution: 2.2 Å

EMDB-50602, PDB-9fnq:
Aerolysin double mutant K238A/K244A in styrene-maleic acid lipid particles
Method: EM (single particle) / Resolution: 2.1 Å

Source
  • aeromonas hydrophila (bacteria)
KeywordsTOXIN / Pore forming toxin Styrene maleic acid lipid particle / pore forming toxin / aerolysin / amphipole reconstitution / cryo-EM

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