6TU4: Plasmodium Actin1 filament

Structure of Plasmodium Actin1 filament. Determined by electron microscopy at 2.6 Å resolution. Released 13 Jan 2021.

Method: Electron microscopy
Resolution: 2.6 Å
Organism: Plasmodium falciparum 3D7
Chains: 5
Atoms: 15,690
Mol. weight: 216.04 kDa
Ligands: ADP, 9UE, MG
Released: 13 Jan 2021

Explore 6TU4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6TU4 contains 121 α-helices and 100 β-strands across 5 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: 25 helices, 20 β-strands

Element	Residues	Length	Sheet
α-helix	6-8	3
β-strand	9-13	5	1
β-strand	17-22	6	1
β-strand	30-33	4	1
β-strand	36-39	4	2
β-strand	43	1	3
β-strand	54-55	2	2
α-helix	57-61	5
α-helix	63-65	3
β-strand	66-69	4	2
β-strand	72-73	2	4
β-strand	76-77	2	4
α-helix	80-88	9
α-helix	89-95	7
β-strand	104-108	5	1
α-helix	114-126	13
β-strand	132-137	6	1
α-helix	138-146	9
β-strand	151-156	6	5
β-strand	161-167	7	5
β-strand	170-171	2	5
α-helix	173-175	3
β-strand	177-179	3	5
α-helix	183-193	11
α-helix	194-197	4
α-helix	204-217	14
α-helix	224-230	7
β-strand	239-242	4	6
β-strand	248-251	4	6
α-helix	254-257	4
α-helix	259-262	4
α-helix	265-267	3
α-helix	275-284	10
α-helix	291-294	4
β-strand	298-301	4	5
α-helix	303-305	3
α-helix	310-321	12
β-strand	330-331	2	5
α-helix	336-338	3
α-helix	339-347	9
α-helix	351-353	3
α-helix	357	1
β-strand	358-359	2	1
α-helix	360-366	7
α-helix	368-373	6

Chain B: 25 helices, 22 β-strands

Element	Residues	Length	Sheet
α-helix	6-8	3
β-strand	9-13	5	7
β-strand	17-22	6	7
β-strand	30-33	4	7
β-strand	36-39	4	8
β-strand	43	1	9
β-strand	54-55	2	8
α-helix	57-61	5
α-helix	63-65	3
β-strand	66-69	4	8
β-strand	72-73	2	10
β-strand	76-77	2	10
α-helix	80-89	10
α-helix	90-94	5
α-helix	99-101	3
β-strand	104-108	5	7
α-helix	114-126	13
β-strand	132-137	6	7
α-helix	138-146	9
β-strand	151-156	6	11
β-strand	161-167	7	11
β-strand	170-171	2	11
α-helix	173-175	3
β-strand	177-179	3	11
α-helix	183-193	11
α-helix	194-197	4
α-helix	204-217	14
β-strand	219	1	12
α-helix	224-231	8
β-strand	239-242	4	13
β-strand	248-251	4	13
α-helix	254-257	4
α-helix	259-262	4
α-helix	265-268	4
α-helix	275-284	10
α-helix	291-294	4
β-strand	298-301	4	11
α-helix	303-305	3
β-strand	308	1	12
α-helix	310-321	12
β-strand	330-331	2	11
α-helix	339-347	9
α-helix	351-355	5
β-strand	358-359	2	7
α-helix	360-366	7
α-helix	368-370	3
α-helix	371-374	4

Chain C: 24 helices, 20 β-strands

Element	Residues	Length	Sheet
α-helix	6-8	3
β-strand	9-13	5	14
β-strand	17-22	6	14
β-strand	30-33	4	14
β-strand	36-39	4	15
β-strand	43	1	5
β-strand	54-55	2	15
α-helix	57-61	5
α-helix	63-65	3
β-strand	66-69	4	15
β-strand	72-73	2	16
β-strand	76-77	2	16
α-helix	80-89	10
α-helix	90-95	6
β-strand	104-108	5	14
α-helix	114-126	13
β-strand	132-137	6	14
α-helix	138-146	9
β-strand	151-156	6	17
β-strand	161-167	7	17
β-strand	170-171	2	17
α-helix	173-175	3
β-strand	177-179	3	17
α-helix	183-193	11
α-helix	194-197	4
α-helix	204-217	14
α-helix	224-231	8
β-strand	239-242	4	18
β-strand	248-251	4	18
α-helix	254-257	4
α-helix	259-262	4
α-helix	265-267	3
α-helix	275-284	10
α-helix	291-295	5
β-strand	298-301	4	17
α-helix	303-305	3
α-helix	310-321	12
β-strand	330-331	2	17
α-helix	339-347	9
α-helix	353-355	3
β-strand	358-359	2	14
α-helix	360-366	7
α-helix	368-370	3
α-helix	371-374	4

Chain D: 23 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	9-13	5	19
β-strand	17-22	6	19
β-strand	30-33	4	19
β-strand	36-39	4	20
β-strand	54-55	2	20
α-helix	57-61	5
α-helix	63-65	3
β-strand	66-69	4	20
β-strand	72-73	2	21
β-strand	76-77	2	21
α-helix	80-89	10
α-helix	90-95	6
β-strand	104-108	5	19
α-helix	114-126	13
β-strand	132-137	6	19
α-helix	138-146	9
β-strand	151-156	6	9
β-strand	161-167	7	9
β-strand	170-171	2	9
α-helix	173-175	3
β-strand	177-179	3	9
α-helix	183-193	11
α-helix	194-197	4
α-helix	204-217	14
α-helix	224-233	10
β-strand	239-242	4	22
β-strand	248-251	4	22
α-helix	254-257	4
α-helix	259-262	4
α-helix	265-267	3
α-helix	275-284	10
α-helix	291-295	5
β-strand	298-301	4	9
α-helix	303-306	4
α-helix	310-321	12
β-strand	330-331	2	9
α-helix	339-347	9
α-helix	351-353	3
β-strand	358-359	2	19
α-helix	360-366	7
α-helix	368-370	3
α-helix	371-374	4

Chain F: 24 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	9-13	5	23
β-strand	17-22	6	23
β-strand	30-33	4	23
β-strand	36-39	4	24
β-strand	54-55	2	24
α-helix	57-61	5
α-helix	63-65	3
β-strand	66-69	4	24
β-strand	72-73	2	25
β-strand	76-77	2	25
α-helix	80-89	10
α-helix	90-94	5
β-strand	104-108	5	23
α-helix	114-126	13
β-strand	132-137	6	23
α-helix	138-146	9
β-strand	151-156	6	3
β-strand	161-167	7	3
β-strand	170-171	2	3
α-helix	173-175	3
β-strand	177-179	3	3
α-helix	183-193	11
α-helix	194-197	4
α-helix	204-217	14
α-helix	224-230	7
α-helix	231-233	3
β-strand	239-242	4	26
β-strand	248-251	4	26
α-helix	254-257	4
α-helix	259-262	4
α-helix	265-268	4
α-helix	275-284	10
α-helix	291-294	4
β-strand	298-301	4	3
α-helix	303-305	3
α-helix	310-321	12
β-strand	330-331	2	3
α-helix	339-347	9
α-helix	357	1
β-strand	358-359	2	23
α-helix	360-366	7
α-helix	367-370	4
α-helix	371-374	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Actin-1	A, B, C, D, F	protein	378	Plasmodium falciparum 3D7	Q8I4X0 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, F), FASTA

>6TU4_1 Actin-1 (chains A, B, C, D, F)
GAMGEEDVQALVVDNGSGNVKAGVAGDDAPRSVFPSIVGRPKNPGIMVGMEEKDAFVGDE
AQTKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRAAPEEHPVLLTEAPLNPKGNRE
RMTQIMFESFNVPAMYVAIQAVLSLYSSGRTTGIVLDSGDGVSHTVPIYEGYALPHAIMR
LDLAGRDLTEYLMKILHERGYGFSTSAEKEIVRDIKEKLCYIALNFDEEMKTSEQSSDIE
KSYELPDGNIITVGNERFRCPEALFQPSFLGKEAAGIHTTTFNSIKKCDVDIRKDLYGNI
VLSGGTTMYEGIGERLTRDITTLAPSTMKIKVVAPPERKYSVWIGGSILSSLSTFQQMWI
TKEEYDESGPSIVHRKCF

Ligands and cofactors

ID	Name	Formula	Copies
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	5
9UE	Jasplakinolide	C36 H45 Br N4 O6	5
MG	Magnesium ion	Mg	5

Primary citation

High-resolution structures of malaria parasite actomyosin and actin filaments. Vahokoski, J., Calder, L.J., Lopez, A.J. et al. PLoS Pathog (2022) 18:e1010408-e1010408. DOI 10.1371/journal.ppat.1010408 · PubMed

Other PDB entries of the same protein (UniProt Q8I4X0 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6I4E 1.22 Å, Crystal Structure of Plasmodium falciparum actin I in the Mg-ADP state
6I4D 1.24 Å, Crystal Structure of Plasmodium falciparum actin I in the Mg-K-ATP/ADP state
4CBU 1.3 Å, Crystal structure of Plasmodium falciparum actin I
5MVV 1.4 Å, Crystal structure of Plasmodium falciparum actin I- gelsolin segment 1 -CdATP complex
6I4H 1.4 Å, Crystal Structure of Plasmodium falciparum actin I (F54Y mutant) in the Ca-ATP state
6I4F 1.5 Å, Crystal Structure of Plasmodium falciparum actin I (A272W mutant) in the Mg-K-ATP/ADP…
6I4J 1.5 Å, Crystal Structure of Plasmodium falciparum actin I (F54Y mutant) in the Mg-ADP state
6I4K 1.83 Å, Crystal Structure of Plasmodium falciparum actin I (G115A mutant) in the Ca-ATP state
6I4L 1.83 Å, Crystal Structure of Plasmodium falciparum actin I (G115A mutant) in the Mg-K-ATP/ADP…
6I4I 1.9 Å, Crystal Structure of Plasmodium falciparum actin I (F54Y mutant) in the Mg-K-ADP-AlFn…
6I4G 2.0 Å, Crystal Structure of Plasmodium falciparum actin I (H74Q) in the Mg-K-ATP state
6TU7 3.1 Å, Structure of PfMyoA decorated Plasmodium Act1 filament

Browse structure collections

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