1PRE: Proaerolysin

Proaerolysin. Determined by X-ray diffraction at 2.8 Å resolution. Released 14 Oct 1996.

Method: X-ray diffraction
Resolution: 2.8 Å
Organism: Aeromonas hydrophila
Chains: 2
Atoms: 7,089
Mol. weight: 103.96 kDa
Released: 14 Oct 1996

Explore 1PRE in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1PRE contains 42 α-helices and 61 β-strands across 2 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.

Chain A: 18 helices, 32 β-strands

Element	Residues	Length	Sheet
β-strand	10-12	3	1
β-strand	23-25	3	1
α-helix	26	1
β-strand	27	1	2
α-helix	28-33	6
α-helix	35-40	6
β-strand	47-49	3	1
β-strand	51	1	2
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	88-90	3
β-strand	91-93	3	3
α-helix	98-106	9
α-helix	109-113	5
α-helix	114-122	9
β-strand	125	1	4
β-strand	140-144	5	3
β-strand	149-153	5	3
β-strand	169-186	18	3
β-strand	191	1	3
β-strand	194-206	13	3
β-strand	212	1	5
β-strand	215-229	15	3
α-helix	235-237	3
β-strand	240	1	3
β-strand	245-246	2	6
α-helix	247-249	3
β-strand	258-259	2	6
α-helix	260	1
α-helix	265-267	3
β-strand	270-281	12	3
β-strand	285	1	5
β-strand	289-321	33	3
β-strand	322	1	4
β-strand	329	1	7
β-strand	338-345	8	3
α-helix	351-353	3
α-helix	355-360	6
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	3
β-strand	417	1	8
β-strand	420-421	2	3
β-strand	442-444	3	3
α-helix	449-454	6
β-strand	458-466	9	3

Chain B: 24 helices, 29 β-strands

Element	Residues	Length	Sheet
α-helix	3-5	3
α-helix	6-8	3
β-strand	10-12	3	9
β-strand	23-25	3	9
α-helix	28-33	6
α-helix	35-39	5
β-strand	47-50	4	9
β-strand	54-57	4	9
α-helix	59-61	3
β-strand	65-67	3	9
β-strand	73-77	5	9
α-helix	80-82	3
α-helix	84-86	3
α-helix	88-90	3
β-strand	91-93	3	10
α-helix	94-95	2
α-helix	98-106	9
α-helix	109-113	5
α-helix	114-122	9
β-strand	125	1	11
β-strand	135	1	8
β-strand	140-145	6	10
β-strand	148-153	6	10
α-helix	167-168	2
β-strand	169-186	18	10
β-strand	192-206	15	10
β-strand	212	1	12
β-strand	215-229	15	10
α-helix	235-238	4
β-strand	239-240	2	10
β-strand	245-246	2	13
α-helix	247-249	3
β-strand	258-259	2	13
α-helix	260	1
α-helix	265-267	3
β-strand	270-281	12	10
β-strand	285	1	12
α-helix	286	1
β-strand	289-321	33	10
β-strand	322	1	11
α-helix	323	1
β-strand	329	1	14
β-strand	338-345	8	10
α-helix	351-353	3
α-helix	355-360	6
β-strand	371	1	14
α-helix	373-380	8
α-helix	382-392	11
β-strand	396-416	21	10
β-strand	420-421	2	10
β-strand	442-444	3	10
α-helix	449-455	7
β-strand	458-466	9	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Proaerolysin	A, B	protein	470	Aeromonas hydrophila	P09167 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1PRE_1 PROAEROLYSIN (chains A, B)
AEPVYPDQLRLFSLGQGVCGDKYRPVNREEAQSVKSNIVGMMGQWQISGLANGWVIMGPG
YNGEIKPGTASNTWCYPTNPVTGEIPTLSALDIPDGDEVDVQWRLVHDSANFIKPTSYLA
HYLGYAWVGGNHSQYVGEDMDVTRDGDGWVIRGNNDGGCDGYRCGDKTAIKVSNFAYNLD
PDSFKHGDVTQSDRQLVKTVVGWAVNDSDTPQSGYDVTLRYDTATNWSKTNTYGLSEKVT
TKNKFKWPLVGETELSIEIAANQSWASQNGGSTTTSLSQSVRPTVPARSKIPVKIELYKA
DISYPYEFKADVSYDLTLSGFLRWGGNAWYTHPDNRPNWNHTFVIGPYKDKASSIRYQWD
KRYIPGEVKWWDWNWTIQQNGLSTMQNNLARVLRPVRAGITGDFSAESQFAGNIEIGAPV
PLAADSKVRRARSVDGAGQGLRLEIPLDAQELSGLGFNNVSLSVTPAANQ

Primary citation

Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states. Parker, M.W., Buckley, J.T., Postma, J.P. et al. Nature (1994) 367:292-295. DOI 10.1038/367292a0 · 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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