5JZH: Aerolysin prepore

Cryo-EM structure of aerolysin prepore. Determined by electron microscopy at 3.9 Å resolution. Released 13 Jul 2016.

Method: Electron microscopy
Resolution: 3.9 Å
Organism: Aeromonas hydrophila
Chains: 14
Atoms: 46,564
Mol. weight: 659.11 kDa
Released: 13 Jul 2016

Explore 5JZH in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5JZH contains 266 α-helices and 448 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, 32 β-strands

Element	Residues	Length	Sheet
α-helix	6-8	3
β-strand	12	1	1
β-strand	20	1	2
β-strand	23	1	2
α-helix	28-32	5
α-helix	35-38	4
α-helix	39-41	3
β-strand	47-51	5	1
β-strand	54-57	4	1
α-helix	59-61	3
β-strand	65-67	3	1
β-strand	73	1	1
β-strand	91-93	3	3
α-helix	98-106	9
α-helix	109-113	5
α-helix	114-123	10
β-strand	125	1	4
β-strand	141-145	5	5
β-strand	148-152	5	5
β-strand	170-172	3	5
β-strand	177-186	10	3
β-strand	190-191	2	3
α-helix	192-194	3
β-strand	195-206	12	6
β-strand	215-219	5	7
β-strand	225-229	5	3
α-helix	235-238	4
β-strand	239-240	2	3
β-strand	246	1	8
β-strand	258	1	8
α-helix	259-260	2
α-helix	265-267	3
β-strand	270-273	4	3
β-strand	278-281	4	7
α-helix	285-286	2
β-strand	289-299	11	6
β-strand	302-312	11	3
β-strand	314-318	5	5
β-strand	322	1	4
α-helix	323	1
β-strand	329	1	9
β-strand	341-345	5	5
α-helix	355-360	6
α-helix	365-367	3
β-strand	371	1	9
α-helix	373-380	8
α-helix	382-392	11
β-strand	396-406	11	3
β-strand	411-416	6	6
β-strand	420-421	2	6
α-helix	423	1

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	424	Aeromonas hydrophila	P09167 (AlphaFold model)

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

>5JZH_1 Aerolysin (chains A, B, C, D, E, F, G, H, I, J, K, L, M, N)
AEPVYPDQLRLFSLGQGVCGDKYRPVNREEAQSVKSNIVGMMGQWQISGLANGWVIMGPG
YNGEIKPGTASNTWCYPTNPVTGEIPTLSALDIPDGDEVDVQWRLVHDSANFIKPTSYLA
HYLGYAWVGGNHSQYVGEDMDVTRDGDGWVIRGNNDGGCDGYRCGDKTAIKVSNFAYNLD
PDSFKHGDVTQSDRQLVKTVVGWAVNDSDTPQSGYDVTLRGDTATNWSKTNTYGLSEKVT
TKNKFKWPLVGETELSIEIAANQSWASQNGGSTTTSLSQSVRPTVPARSKIPVKIELYKA
DISYPYEFKADVSYDLTLSGFLRWGGNAWYTHPDNRPNWNHTFVIGPYKDKASSIRYQWD
KRYIPGEVKWWDWNWTIQQNGLSTMQNNLARVLRPVRAGITGDFSAESQFAGNIEIGAPV
PLAA

Primary citation

Cryo-EM structure of aerolysin variants reveals a novel protein fold and the pore-formation process. Iacovache, I., De Carlo, S., Cirauqui, N. et al. Nat Commun (2016) 7:12062-12062. DOI 10.1038/ncomms12062 · 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
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

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