9GXJ: Aerolysin

Aerolysin E254A/E258A in styrene-maleic acid lipid particles. Determined by electron microscopy at 2.3 Å resolution. Released 8 Oct 2025.

Method: Electron microscopy
Resolution: 2.3 Å
Organism: Aeromonas hydrophila
Chains: 7
Atoms: 22,365
Mol. weight: 329.48 kDa
Released: 8 Oct 2025

Explore 9GXJ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9GXJ contains 98 α-helices and 168 β-strands across 7 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chains A, B, C, D, E, F and G: 14 helices, 24 β-strands

Element	Residues	Length	Sheet
α-helix	6-8	3
β-strand	10-12	3	1
β-strand	25	1	1
α-helix	28-33	6
α-helix	35-40	6
β-strand	48-49	2	1
β-strand	54-56	3	1
α-helix	59-61	3
β-strand	65-67	3	1
β-strand	73-75	3	1
α-helix	84-86	3
α-helix	88-90	3
β-strand	91-96	6	2
α-helix	98-106	9
α-helix	109-113	5
α-helix	114-123	10
β-strand	125	1	3
β-strand	140-144	5	2
β-strand	149-153	5	2
β-strand	169-179	11	2
β-strand	185-186	2	2
β-strand	190-206	17	2
β-strand	212	1	4
β-strand	215-243	29	5
β-strand	253-281	29	5
β-strand	285	1	4
β-strand	289-321	33	2
β-strand	322	1	3
β-strand	329	1	6
β-strand	338-345	8	2
α-helix	351-353	3
α-helix	355-360	6
α-helix	365-367	3
β-strand	371	1	6
α-helix	373-380	8
α-helix	382-392	11
β-strand	396-416	21	2
β-strand	420-421	2	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Aerolysin	A, B, C, D, E, F, G	protein	424	Aeromonas hydrophila	P09167 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E, F, G), FASTA

>9GXJ_1 Aerolysin (chains A, B, C, D, E, F, G)
AEPVYPDQLRLFSLGQGVCGDKYRPVNREEAQSVKSNIVGMMGQWQISGLANGWVIMGPG
YNGEIKPGTASNTWCYPTNPVTGEIPTLSALDIPDGDEVDVQWRLVHDSANFIKPTSYLA
HYLGYAWVGGNHSQYVGEDMDVTRDGDGWVIRGNNDGGCDGYRCGDKTAIKVSNFAYNLD
PDSFKHGDVTQSDRQLVKTVVGWAVNDSDTPQSGYDVTLRYDTATNWSKTNTYGLSEKVT
TKNKFKWPLVGETALSIAIAANQSWASQNGGSTTTSLSQSVRPTVPARSKIPVKIELYKA
DISYPYEFKADVSYDLTLSGFLRWGGNAWYTHPDNRPNWNHTFVIGPYKDKASSIRYQWD
KRYIPGEVKWWDWNWTIQQNGLSTMQNNLARVLRPVRAGITGDFSAESQFAGNIEIGAPV
PLAA

Primary citation

Lumen charge governs gated ion transport in beta-barrel nanopores. Mayer, S.F., Mitsioni, M.F., Robin, P. et al. Nat Nanotechnol (2026) 21:116-124. DOI 10.1038/s41565-025-02052-6 · PubMed

Other PDB entries of the same protein (UniProt P09167 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3G4N 2.1 Å, Crystal structure of the activated aerolysin mutant H132D
9FNQ 2.1 Å, Aerolysin double mutant K238A/K244A in styrene-maleic acid lipid particles
3C0N 2.2 Å, Crystal structure of the proaerolysin mutant Y221G at 2.2 A
9FM6 2.2 Å, Aerolysin Wildtype in styrene-maleic acid lipid particles
9FML 2.2 Å, Aerolysin heptamer in membrane inserted form reconstituted in amphipoles.
9FMX 2.2 Å, Aerolysin Y221G - prepore
9FNP 2.2 Å, Aerolysin mutant K238A in styrene-maleic acid lipid particles
3G4O 2.3 Å, Crystal structure of the activated aerolysin mutant H132N
9IGN 2.3 Å, Aerolysin E254A/E258A in styrene-maleic acid lipid particles
1Z52 2.38 Å, Proaerolysin Mutant W373L
3C0O 2.5 Å, Crystal structure of the proaerolysin mutant Y221G complexed with mannose-6-phosphate
1PRE 2.8 Å, Proaerolysin

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