8RBF: Post-powerstroke actomyosin-5a complex

CryoEM structure of the post-powerstroke actomyosin-5a complex. Determined by electron microscopy at 4.2 Å resolution. Released 11 Dec 2024.

Method: Electron microscopy
Resolution: 4.2 Å
Organisms: Mus musculus, Oryctolagus cuniculus
Chains: 4
Atoms: 14,790
Mol. weight: 214.81 kDa
Ligands: ADP, MG
Released: 11 Dec 2024

Explore 8RBF in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8RBF contains 95 α-helices and 89 β-strands across 4 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: 38 helices, 27 β-strands

Element	Residues	Length	Sheet
β-strand	12-17	6	1
β-strand	21-27	7	1
β-strand	37-42	6	1
β-strand	45-51	7	1
α-helix	52-53	2
α-helix	58-60	3
β-strand	61-62	2	1
α-helix	63-65	3
β-strand	73	1	2
α-helix	74-76	3
α-helix	82-94	13
β-strand	100-103	4	2
β-strand	106-110	5	2
α-helix	121-127	7
α-helix	136	1
α-helix	139-153	15
β-strand	157-163	7	2
α-helix	169-182	14
α-helix	192-207	16
β-strand	208-211	4	3
β-strand	214-218	5	3
β-strand	221-228	8	2
β-strand	234-242	9	2
α-helix	247-249	3
β-strand	259	1	3
α-helix	260-268	9
α-helix	272-276	5
α-helix	286-289	4
α-helix	296	1
α-helix	301-315	15
α-helix	319-337	19
β-strand	341-342	2	4
β-strand	348-349	2	4
α-helix	355-364	10
α-helix	368-376	9
β-strand	377-381	5	5
β-strand	386-390	5	5
α-helix	393-423	31
α-helix	428-429	2
β-strand	431-436	6	2
β-strand	447	1	6
α-helix	449-479	31
α-helix	484-486	3
α-helix	488-489	2
α-helix	493-500	8
α-helix	505-514	10
α-helix	520-531	12
β-strand	539	1	6
β-strand	547-551	5	6
β-strand	556-560	5	6
α-helix	564-568	5
α-helix	574-581	8
α-helix	588-591	4
α-helix	627-630	4
α-helix	635-652	18
β-strand	654-661	8	2
α-helix	674-683	10
α-helix	686-695	10
β-strand	700-702	3	7
α-helix	703-710	8
α-helix	723-734	12
α-helix	738-740	3
β-strand	741-743	3	7
β-strand	747-750	4	7
α-helix	754-766	13

Chain B: 19 helices, 20 β-strands

Element	Residues	Length	Sheet
α-helix	7-8	2
β-strand	9-12	4	8
β-strand	18-22	5	8
β-strand	30-32	3	8
β-strand	36-39	4	9
β-strand	54-55	2	9
α-helix	57-60	4
β-strand	63	1	9
β-strand	66-69	4	9
β-strand	72-73	2	10
β-strand	76-77	2	10
α-helix	80-88	9
α-helix	89-94	6
β-strand	104-108	5	8
α-helix	114-126	13
β-strand	132-137	6	8
α-helix	138-146	9
β-strand	151-156	6	11
β-strand	161-167	7	11
β-strand	170-171	2	11
β-strand	177-179	3	11
α-helix	183-195	13
α-helix	204-217	14
α-helix	224-233	10
β-strand	239-242	4	12
β-strand	248-251	4	12
α-helix	254-260	7
α-helix	265-268	4
α-helix	273-274	2
α-helix	275-285	11
α-helix	291-295	5
β-strand	298-301	4	11
α-helix	303-305	3
α-helix	310-321	12
β-strand	330-331	2	11
α-helix	339-349	11
β-strand	358-359	2	8
α-helix	360-366	7
α-helix	370-375	6

Chain C: 19 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	8-11	4	13
β-strand	17-21	5	13
β-strand	29-31	3	13
β-strand	35-38	4	14
β-strand	53-54	2	14
α-helix	56-59	4
β-strand	62	1	14
β-strand	65-68	4	14
β-strand	71-72	2	15
β-strand	75-76	2	15
α-helix	79-87	9
α-helix	88-93	6
β-strand	103-107	5	13
α-helix	113-125	13
β-strand	131-136	6	13
α-helix	137-145	9
β-strand	151-155	5	16
β-strand	160-163	4	16
β-strand	165-166	2	17
β-strand	169-170	2	17
β-strand	176-178	3	16
α-helix	182-194	13
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	18
β-strand	247-250	4	18
α-helix	253-259	7
α-helix	264-267	4
α-helix	272-273	2
α-helix	274-284	11
α-helix	290-294	5
β-strand	297-300	4	16
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	16
α-helix	339-348	10
α-helix	352-354	3
β-strand	357-358	2	13
α-helix	359-364	6
α-helix	369-374	6

Chain D: 19 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	8-11	4	19
β-strand	17-21	5	19
β-strand	29-31	3	19
β-strand	35-38	4	20
β-strand	41-42	2	11
β-strand	53-54	2	20
α-helix	56-59	4
β-strand	62	1	20
β-strand	65-68	4	20
β-strand	71-72	2	21
β-strand	75-76	2	21
α-helix	79-87	9
α-helix	88-93	6
β-strand	103-107	5	19
α-helix	113-125	13
β-strand	131-136	6	19
α-helix	137-145	9
β-strand	150-155	6	22
β-strand	160-166	7	22
β-strand	169-170	2	22
β-strand	176-178	3	22
α-helix	182-194	13
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	23
β-strand	247-250	4	23
α-helix	253-259	7
α-helix	264-267	4
α-helix	272-273	2
α-helix	274-283	10
α-helix	287-294	8
β-strand	297-300	4	22
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	22
α-helix	335-337	3
α-helix	338-346	9
β-strand	357-358	2	19
α-helix	359-365	7
α-helix	369-374	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Unconventional myosin-Va	A	protein	759	Mus musculus	Q99104 (AlphaFold model)
Actin, alpha skeletal muscle	B, C, D	protein	376	Oryctolagus cuniculus	P68135 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>8RBF_1 Unconventional myosin-Va (chains A)
ELYTKFARVWIPDPEEVWKSAELLKDYKPGDKVLLLHLEEGKDLEYRLDPKTGELPHLRN
PDILVGENDLTALSYLHEPAVLHNLRVRFIDSKLIYTYCGIVLVAINPYEQLPIYGEDII
NAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGESGAGKTVSAKYAMRYFATVS
GSASEANVEEKVLASNPIMESIGNAKTTRNDNASRFGKYIEIGFDKRYRIIGANMRTYLL
EKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADSFHYTKQGGSPMIEGVDDAKE
MAHTRQACTLLGISESYQMGIFRILAGILHLGNVGFASRDSDSCTIPPKHEPLTIFCDLM
GVDYEEMCHWLCHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDHVNQALH
SAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPW
TLIDFYDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRMS
NKAFIIKHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQAISPTSATSSG
RTPLTRVPVKPTKGRPGQTAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKF
PFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQKDVLGDRKQTCK
NVLEKLILDKDKYQFGKTKIFFRAGQVAYLEKLRADKLR

Sequence of entity 2 (B, C, D), FASTA

>8RBF_2 Actin, alpha skeletal muscle (chains B, C, D)
XDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQ
SKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKM
TQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLD
LAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKS
YELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVM
SGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITK
QEYDEAGPSIVHRKCF

Ligands and cofactors

ID	Name	Formula	Copies
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	4
MG	Magnesium ion	Mg	4

Primary citation

Swinging lever mechanism of myosin directly shown by time-resolved cryo-EM. Klebl, D.P., McMillan, S.N., Risi, C. et al. Nature (2025) 642:519-526. DOI 10.1038/s41586-025-08876-5 · PubMed

Other PDB entries of the same protein (UniProt Q99104 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6KU0 1.6 Å, Crystal structure of MyoVa-GTD in complex with MICAL1-GTBM
4KP3 2.4 Å, Crystal Structure of MyoVa-GTD in Complex with Two Cargos
3WB8 2.5 Å, Crystal Structure of MyoVa-GTD
2IX7 2.5 Å, Structure of apo-calmodulin bound to unconventional myosin V
4ZLK 2.5 Å, Crystal structure of mouse myosin-5a in complex with calcium-bound calmodulin
8R9V 4.4 Å, CryoEM structure of the primed actomyosin-5a complex
7YV9 4.78 Å, Cryo-EM structure of full-length Myosin Va in the autoinhibited state
8RBG 4.9 Å, CryoEM structure of primed myosin-5a (ADP-Pi state)
8OF8 7.5 Å, Cryo-EM structure of actomyosin-5a-S1 with the full-length lever (nucleotide free)

Browse structure collections

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