1Z52: Proaerolysin Mutant W373L

Name: PDB 1Z52: Proaerolysin Mutant W373L
Published: 2006-03-07
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: toxin

Proaerolysin Mutant W373L. Determined by X-ray diffraction at 2.38 Å resolution. Released 7 Mar 2006.

Method: X-ray diffraction
Resolution: 2.38 Å
Organism: Aeromonas hydrophila
Chains: 2
Atoms: 7,179
Mol. weight: 103.81 kDa
Released: 7 Mar 2006

Explore 1Z52 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1Z52 contains 40 α-helices and 60 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: 19 helices, 29 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	26-27	2
α-helix	28-33	6
α-helix	35-39	5
β-strand	47-50	4	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	84-86	3
α-helix	88-90	3
β-strand	91-93	3	2
α-helix	98-106	9
α-helix	109-113	5
α-helix	114-122	9
β-strand	125	1	3
β-strand	140-144	5	2
β-strand	149-153	5	2
α-helix	167-168	2
β-strand	169-186	18	2
β-strand	194-206	13	2
β-strand	212	1	4
β-strand	215-229	15	2
α-helix	234-237	4
β-strand	239-240	2	2
β-strand	245-246	2	5
α-helix	247-249	3
β-strand	258-259	2	5
α-helix	260	1
α-helix	265-267	3
β-strand	270-281	12	2
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	355-360	6
β-strand	371	1	6
α-helix	373-380	8
α-helix	382-392	11
β-strand	396-411	16	2
β-strand	415-416	2	2
β-strand	420-421	2	2
β-strand	442-444	3	2
α-helix	449-454	6
β-strand	458-466	9	2

Chain B: 21 helices, 31 β-strands

Element	Residues	Length	Sheet
α-helix	6-8	3
β-strand	10-12	3	7
β-strand	23-25	3	7
α-helix	28-33	6
α-helix	35-39	5
β-strand	47-50	4	7
β-strand	54-57	4	7
α-helix	59-61	3
β-strand	65-67	3	7
β-strand	73-77	5	7
α-helix	80-82	3
α-helix	84-86	3
α-helix	88-90	3
β-strand	91-93	3	8
α-helix	94-95	2
α-helix	98-106	9
α-helix	109-113	5
α-helix	114-122	9
β-strand	125	1	9
β-strand	140-145	6	8
β-strand	148-153	6	8
β-strand	169-186	18	8
β-strand	191-205	15	8
β-strand	212	1	10
β-strand	215-222	8	11
β-strand	224-229	6	8
α-helix	235-238	4
β-strand	239-240	2	8
β-strand	245-246	2	12
α-helix	247-249	3
β-strand	258-259	2	12
α-helix	260	1
α-helix	265-267	3
β-strand	270-274	5	8
β-strand	277-281	5	11
β-strand	285	1	10
α-helix	286	1
β-strand	289-321	33	8
β-strand	322	1	9
β-strand	329	1	13
β-strand	338-345	8	8
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	8
β-strand	415-416	2	8
β-strand	420-421	2	8
β-strand	442-444	3	8
α-helix	449-455	7
β-strand	458-466	9	11

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

>1Z52_1 Aerolysin (chains A, B)
AEPVYPDQLRLFSLGQGVCGDKYRPVNREEAQSVKSNIVGMMGQWQISGLANGWVIMGPG
YNGEIKPGTASNTWCYPTNPVTGEIPTLSALDIPDGDEVDVQWRLVHDSANFIKPTSYLA
HYLGYAWVGGNHSQYVGEDMDVTRDGDGWVIRGNNDGGCDGYRCGDKTAIKVSNFAYNLD
PDSFKHGDVTQSDRQLVKTVVGWAVNDSDTPQSGYDVTLRYDTATNWSKTNTYGLSEKVT
TKNKFKWPLVGETELSIEIAANQSWASQNGGSTTTSLSQSVRPTVPARSKIPVKIELYKA
DISYPYEFKADVSYDLTLSGFLRWGGNAWYTHPDNRPNWNHTFVIGPYKDKASSIRYQWD
KRYIPGEVKWWDLNWTIQQNGLSTMQNNLARVLRPVRAGITGDFSAESQFAGNIEIGAPV
PLAADSKVRRARSVDGAGQGLRLEIPLDAQELSGLGFNNVSLSVTPAANQ

Primary citation

Crystal Structure of Proaerolysin at 2.3 A Resolution and Structural Analyses of Single-site Mutants as a Basis for Understanding Membrane Insertion of the Toxin. Parker, M.W., Feil, S.C., Tang, J.W. To be published.

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
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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