3G4O: Activated aerolysin mutant H132N

Name: PDB 3G4O: Crystal structure of the activated aerolysin mutant H132N
Published: 2010-02-09
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: toxin

Crystal structure of the activated aerolysin mutant H132N. Determined by X-ray diffraction at 2.3 Å resolution. Released 9 Feb 2010.

Method: X-ray diffraction
Resolution: 2.3 Å
Organism: Aeromonas hydrophila
Chains: 2
Atoms: 7,165
Mol. weight: 103.91 kDa
Released: 9 Feb 2010

Explore 3G4O in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3G4O contains 43 α-helices and 57 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: 24 helices, 28 β-strands

Element	Residues	Length	Sheet
α-helix	3-5	3
α-helix	6-8	3
β-strand	10-12	3	1
β-strand	23-25	3	1
α-helix	26-27	2
α-helix	28-33	6
α-helix	35-39	5
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	84-86	3
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	169-186	18	2
β-strand	192-206	15	2
β-strand	212-213	2	4
β-strand	221-222	2	5
β-strand	224-229	6	2
α-helix	235-237	3
β-strand	239-240	2	2
β-strand	245-246	2	6
α-helix	247-248	2
β-strand	258-259	2	6
α-helix	260	1
α-helix	265-267	3
β-strand	270-273	4	2
β-strand	276-277	2	5
β-strand	284-285	2	4
α-helix	286	1
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	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
α-helix	394-395	2
β-strand	396-416	21	2
β-strand	420-421	2	2
α-helix	449-453	5

Chain B: 19 helices, 29 β-strands

Element	Residues	Length	Sheet
α-helix	6-8	3
β-strand	10-12	3	8
β-strand	23-25	3	8
α-helix	26-27	2
α-helix	28-33	6
α-helix	35-39	5
β-strand	47-49	3	8
β-strand	54-57	4	8
α-helix	59-61	3
β-strand	65-67	3	8
β-strand	73-77	5	8
α-helix	80-82	3
α-helix	88-90	3
β-strand	91-93	3	9
α-helix	98-106	9
α-helix	109-113	5
α-helix	114-123	10
β-strand	125	1	10
β-strand	140-145	6	9
β-strand	148-153	6	9
β-strand	169-186	18	9
β-strand	192-206	15	9
β-strand	212	1	11
β-strand	216-229	14	9
α-helix	235-238	4
β-strand	239-240	2	9
β-strand	245-246	2	12
β-strand	258-259	2	12
α-helix	260	1
α-helix	265-267	3
β-strand	270-281	12	9
β-strand	285	1	11
β-strand	289-321	33	9
β-strand	322	1	10
α-helix	323	1
β-strand	329	1	13
β-strand	338-345	8	9
α-helix	351-353	3
α-helix	355-360	6
β-strand	371	1	13
α-helix	373-380	8
α-helix	382-392	11
β-strand	396-411	16	9
β-strand	415-416	2	9
β-strand	420-421	2	9
β-strand	441-444	4	9
α-helix	449-453	5
β-strand	457-465	9	9

Molecules and chains

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

Sequence of entity 1 (A, B), FASTA

>3G4O_1 Aerolysin (chains A, B)
AEPVYPDQLRLFSLGQGVCGDKYRPVNREEAQSVKSNIVGMMGQWQISGLANGWVIMGPG
YNGEIKPGTASNTWCYPTNPVTGEIPTLSALDIPDGDEVDVQWRLVHDSANFIKPTSYLA
HYLGYAWVGGNNSQYVGEDMDVTRDGDGWVIRGNNDGGCDGYRCGDKTAIKVSNFAYNLD
PDSFKHGDVTQSDRQLVKTVVGWAVNDSDTPQSGYDVTLRYDTATNWSKTNTYGLSEKVT
TKNKFKWPLVGETELSIEIAANQSWASQNGGSTTTSLSQSVRPTVPARSKIPVKIELYKA
DISYPYEFKADVSYDLTLSGFLRWGGNAWYTHPDNRPNWNHTFVIGPYKDKASSIRYQWD
KRYIPGEVKWWDWNWTIQQNGLSTMQNNLARVLRPVRAGITGDFSAESQFAGNIEIGAPV
PLAADSKVRRARSVDGAGQGLRLEIPLDAQELSGLGFNNVSLSVTPAANQ

Primary citation

Dual chaperone role of the C-terminal propeptide in folding and oligomerization of the pore-forming toxin aerolysin. Iacovache, I., Degiacomi, M.T., Pernot, L. et al. PLoS Pathog (2011) 7:e1002135-e1002135. DOI 10.1371/journal.ppat.1002135 · 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
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

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