9GXJ
Aerolysin E254A/E258A in styrene-maleic acid lipid particles
This is a non-PDB format compatible entry.
Summary for 9GXJ
| Entry DOI | 10.2210/pdb9gxj/pdb |
| Related | 5JZT 9FM6 |
| EMDB information | 51664 |
| 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 | 329483.60 |
| Authors | Anton, J.S.,Bada Juarez, J.F.,Marcaida, M.J.,Dal Peraro, M. (deposition date: 2024-09-30, release date: 2025-10-08, Last modification date: 2025-12-03) |
| Primary citation | Mayer, S.F.,Mitsioni, M.F.,Robin, P.,van den Heuvel, L.,Ronceray, N.,Marcaida, M.J.,Abriata, L.A.,Krapp, L.F.,Anton, J.S.,Soussou, S.,Jeanneret-Grosjean, J.,Fulciniti, A.,Moller, A.,Vacle, S.,Feletti, L.,Brinkerhoff, H.,Laszlo, A.H.,Gundlach, J.H.,Emmerich, T.,Dal Peraro, M.,Radenovic, A. Lumen charge governs gated ion transport in beta-barrel nanopores. Nat Nanotechnol, 2025 Cited by PubMed Abstract: β-Barrel nanopores are involved in crucial biological processes, from ATP export in mitochondria to bacterial resistance, and represent a promising platform for emerging sequencing technologies. However, in contrast to ion channels, the understanding of the fundamental principles governing ion transport through these nanopores remains largely unexplored. Here we integrate experimental, numerical and theoretical approaches to elucidate ion transport mechanisms in β-barrel nanopores. We identify and characterize two distinct nonlinear phenomena: open-pore rectification and gating. Through extensive mutation analysis of aerolysin nanopores, we demonstrate that open-pore rectification is caused by ionic accumulation driven by the distribution of lumen charges. In addition, we provide converging evidence suggesting that gating is controlled by electric fields dissociating counterions from lumen charges, promoting local structural deformations. Our findings establish a rigorous framework for characterizing and understanding ion transport processes in protein-based nanopores, enabling the design of adaptable nanofluidic biotechnologies. We illustrate this by optimizing an aerolysin mutant for computing applications. PubMed: 41219410DOI: 10.1038/s41565-025-02052-6 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.3 Å) |
Structure validation
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