9FMX: Aerolysin Y221G - prepore

Aerolysin Y221G - prepore. Determined by electron microscopy at 2.2 Å resolution. Released 12 Feb 2025.

Method: Electron microscopy
Resolution: 2.2 Å
Organism: Aeromonas hydrophila
Chains: 14
Atoms: 46,550
Mol. weight: 741.24 kDa
Released: 12 Feb 2025

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

Secondary structure: helices and β-sheets

9FMX contains 266 α-helices and 434 β-strands across 14 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, G, H, I, J, K, L, M and N: 19 helices, 31 β-strands

Element	Residues	Length	Sheet
α-helix	6-8	3
β-strand	10-12	3	1
β-strand	23-25	3	1
α-helix	28-33	6
α-helix	35-40	6
β-strand	47-49	3	1
β-strand	54-57	4	1
α-helix	59-61	3
β-strand	65-67	3	1
β-strand	73-77	5	1
α-helix	80-82	3
α-helix	84-90	7
β-strand	91-93	3	2
α-helix	98-106	9
α-helix	109-113	5
α-helix	114-123	10
β-strand	125	1	3
β-strand	140-145	6	2
β-strand	148-153	6	2
β-strand	169-177	9	2
β-strand	180-186	7	2
β-strand	190-191	2	2
α-helix	192-194	3
β-strand	195-206	12	2
β-strand	212	1	4
β-strand	215-220	6	2
β-strand	222-229	8	2
α-helix	235-238	4
β-strand	239	1	2
β-strand	245-246	2	5
α-helix	247-249	3
β-strand	250	1	6
β-strand	253	1	6
β-strand	258-259	2	5
α-helix	260	1
β-strand	270-281	12	2
β-strand	285	1	4
β-strand	289-321	33	2
β-strand	322	1	3
α-helix	323	1
β-strand	329	1	7
β-strand	338-345	8	2
α-helix	355-360	6
α-helix	361-363	3
α-helix	365-367	3
β-strand	371	1	7
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, H, I, J, K, L, M, N	protein	478	Aeromonas hydrophila	P09167 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E, F, G, H, I, J, K, L, M, N), FASTA

>9FMX_1 Aerolysin (chains A, B, C, D, E, F, G, H, I, J, K, L, M, N)
AEPVYPDQLRLFSLGQGVCGDKYRPVNREEAQSVKSNIVGMMGQWQISGLANGWVIMGPG
YNGEIKPGTASNTWCYPTNPVTGEIPTLSALDIPDGDEVDVQWRLVHDSANFIKPTSYLA
HYLGYAWVGGNHSQYVGEDMDVTRDGDGWVIRGNNDGGCDGYRCGDKTAIKVSNFAYNLD
PDSFKHGDVTQSDRQLVKTVVGWAVNDSDTPQSGYDVTLRGDTATNWSKTNTYGLSEKVT
TKNKFKWPLVGETELSIEIAANQSWASQNGGSTTTSLSQSVRPTVPARSKIPVKIELYKA
DISYPYEFKADVSYDLTLSGFLRWGGNAWYTHPDNRPNWNHTFVIGPYKDKASSIRYQWD
KRYIPGEVKWWDWNWTIQQNGLSTMQNNLARVLRPVRAGITGDFSAESQFAGNIEIGAPV
PLAADSKVRRARSVDGAGQGLRLEIPLDAQELSGLGFNNVSLSVTPAANQLEHHHHHH

Primary citation

Aerolysin Nanopore Structures Revealed at High Resolution in a Lipid Environment. Anton, J.S., Iacovache, I., Bada Juarez, J.F. et al. J Am Chem Soc (2025) 147:4984-4992. DOI 10.1021/jacs.4c14288 · 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.
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
9GXJ 2.3 Å, Aerolysin E254A/E258A in styrene-maleic acid lipid particles
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

Browse structure collections

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