8OF8: Actomyosin-5a-S1 with the full-length lever

Cryo-EM structure of actomyosin-5a-S1 with the full-length lever (nucleotide free). Determined by electron microscopy at 7.5 Å resolution. Released 25 Sept 2024.

Method: Electron microscopy
Resolution: 7.5 Å
Organisms: Mus musculus, Oryctolagus cuniculus
Chains: 10
Atoms: 15,859
Mol. weight: 332.55 kDa
Released: 25 Sept 2024

Explore 8OF8 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8OF8 contains 176 α-helices and 112 β-strands across 10 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: 9 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	6-19	14
β-strand	26-28	3	1
α-helix	29-31	3
α-helix	32-38	7
α-helix	45-55	11
β-strand	62-64	3	1
α-helix	65-76	12
α-helix	82-90	9
β-strand	99-101	3	2
α-helix	102-110	9
α-helix	118-128	11
β-strand	135-137	3	2
α-helix	139-145	7

Chain B: 10 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	6-16	11
β-strand	26-28	3	3
α-helix	29-31	3
α-helix	32-38	7
α-helix	45-55	11
β-strand	62-64	3	3
α-helix	65-74	10
α-helix	77-80	4
α-helix	82-92	11
β-strand	100-101	2	4
α-helix	102-111	10
α-helix	118-127	10
β-strand	130	1	4
β-strand	135-136	2	4
α-helix	138-145	8

Chain C: 9 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	6-17	12
β-strand	26-28	3	5
α-helix	29-31	3
α-helix	32-38	7
α-helix	45-52	8
β-strand	62-64	3	5
α-helix	65-75	11
α-helix	82-90	9
β-strand	93	1	6
β-strand	99-101	3	6
α-helix	102-110	9
α-helix	118-128	11
β-strand	135-137	3	6
α-helix	138-145	8

Chain D: 10 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	6-16	11
β-strand	26-28	3	7
α-helix	29-31	3
α-helix	32-38	7
α-helix	45-53	9
β-strand	62-64	3	7
α-helix	65-74	10
α-helix	84-90	7
β-strand	99-101	3	8
α-helix	102-111	10
α-helix	115-117	3
α-helix	118-128	11
β-strand	135-137	3	8
α-helix	138-144	7

Chain E: 8 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	6-16	11
β-strand	26-28	3	9
α-helix	29-38	10
α-helix	45-55	11
β-strand	62-64	3	9
α-helix	65-76	12
α-helix	83-90	8
β-strand	93	1	10
β-strand	99-101	3	10
α-helix	102-110	9
α-helix	118-128	11
β-strand	135-137	3	10
α-helix	138-145	8

Chain F: 8 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	6-17	12
β-strand	26-28	3	11
α-helix	30-39	10
α-helix	45-53	9
β-strand	62-64	3	11
α-helix	65-74	10
α-helix	82-92	11
β-strand	99-101	3	12
α-helix	102-111	10
α-helix	118-128	11
β-strand	135-137	3	12
α-helix	139-143	5

Chain J: 29 helices, 21 β-strands

Element	Residues	Length	Sheet
α-helix	6-7	2
β-strand	8-11	4	13
β-strand	16-21	6	13
β-strand	22	1	14
β-strand	24	1	14
β-strand	29-32	4	13
β-strand	35-38	4	15
α-helix	41-42	2
β-strand	53-54	2	15
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	15
β-strand	71-72	2	16
β-strand	75-76	2	16
α-helix	79-87	9
α-helix	88-94	7
α-helix	98-100	3
β-strand	103-107	5	13
α-helix	113-121	9
α-helix	122-126	5
β-strand	131-136	6	13
α-helix	137-144	8
β-strand	150-155	6	17
β-strand	160-166	7	17
β-strand	169-170	2	17
α-helix	172-174	3
β-strand	176-178	3	17
α-helix	182-193	12
α-helix	194-196	3
α-helix	203-216	14
α-helix	223-232	10
α-helix	234-236	3
β-strand	238-241	4	18
β-strand	247-250	4	18
α-helix	253-259	7
α-helix	264-267	4
α-helix	274-284	11
α-helix	287-289	3
α-helix	290-295	6
β-strand	297-300	4	17
α-helix	302-304	3
α-helix	309-318	10
β-strand	329-330	2	17
α-helix	333-337	5
α-helix	338-346	9
α-helix	350-355	6
β-strand	357-358	2	13
α-helix	359-365	7
α-helix	367-369	3
α-helix	370-373	4

Chain K: 28 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	6-7	2
β-strand	8-14	7	19
β-strand	16-21	6	19
β-strand	29-32	4	19
β-strand	35-38	4	20
α-helix	41-42	2
β-strand	53-54	2	20
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	20
β-strand	71-72	2	21
β-strand	75-76	2	21
α-helix	79-88	10
α-helix	89-94	6
β-strand	103-107	5	19
α-helix	113-121	9
α-helix	122-126	5
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
α-helix	172-174	3
β-strand	177-178	2	22
α-helix	182-193	12
α-helix	194-196	3
α-helix	203-215	13
α-helix	223-232	10
α-helix	234-236	3
β-strand	238-241	4	23
α-helix	246	1
β-strand	247-250	4	23
α-helix	253-256	4
α-helix	258-262	5
α-helix	264-267	4
α-helix	274-283	10
α-helix	290-295	6
β-strand	296-300	5	22
α-helix	302-304	3
α-helix	309-318	10
β-strand	328-330	3	22
α-helix	335-337	3
α-helix	338-346	9
α-helix	350-354	5
β-strand	357-358	2	19
α-helix	359-365	7
α-helix	369-373	5

2 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Calmodulin-1	A, B, C, D, E, F	protein	148	Mus musculus	P0DP26 (AlphaFold model)
Actin, alpha skeletal muscle	J, K, L	protein	375	Oryctolagus cuniculus	P68135 (AlphaFold model)
Unconventional myosin-Va	M	protein	915	Mus musculus	Q99104 (AlphaFold model)

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

>8OF8_1 Calmodulin-1 (chains A, B, C, D, E, F)
ADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGN
GTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEE
VDEMIREADIDGDGQVNYEEFVQMMTAK

Sequence of entity 2 (J, K, L), FASTA

>8OF8_2 Actin, alpha skeletal muscle (chains J, K, L)
DEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQS
KRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMT
QIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDL
AGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSY
ELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMS
GGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQ
EYDEAGPSIVHRKCF

Sequence of entity 3 (M), FASTA

>8OF8_3 Unconventional myosin-Va (chains M)
MAASELYTKFARVWIPDPEEVWKSAELLKDYKPGDKVLLLHLEEGKDLEYRLDPKTGELP
HLRNPDILVGENDLTALSYLHEPAVLHNLRVRFIDSKLIYTYCGIVLVAINPYEQLPIYG
EDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGESGAGKTVSAKYAMRYF
ATVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMR
TYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADSFHYTKQGGSPMIEGVD
DAKEMAHTRQACTLLGISESYQMGIFRILAGILHLGNVGFASRDSDSCTIPPKHEPLTIF
CDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDHVN
QALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKE
QIPWTLIDFYDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEK
PRMSNKAFIIKHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAIS
PTSATSSGRTPLTRVPVKPTKGRPGQTAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRC
IKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQKDVL
GDRKQTCKNVLEKLILDKDKYQFGKTKIFFRAGQVAYLEKLRADKLRAACIRIQKTIRGW
LLRKRYLCMQRAAITVQRYVRGYQARCYAKFLRRTKAATTIQKYWRMYVVRRRYKIRRAA
TIVIQSYLRGYLTRNRYRKILREYKAVIIQKRVRGWLARTHYKRTMKAIVYLQCCFRRMM
AKRELKKDYKDDDDK

Primary citation

Exploiting cryo-EM structures of actomyosin-5a to reveal the physical properties of its lever. Gravett, M.S.C., Klebl, D.P., Harlen, O.G. et al. Structure (2024) 32:2316-2324.e6. DOI 10.1016/j.str.2024.09.025 · PubMed

Other PDB entries of the same protein (UniProt P0DP26 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7CQP 1.9 Å, Complex of TRPC4 and Calmodulin_Nlobe
3WFN 1.95 Å, Crystal Structure of Nav1.6 IQ motif in complex with apo-CaM
4HEX 2.0 Å, A novel conformation of calmodulin
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
4E53 2.69 Å, Calmodulin and Nm peptide complex
4E50 2.7 Å, Calmodulin and Ng peptide complex
9CFV 2.7 Å, Cryo-EM structure of delta-NTR myosin-1c bound to F-actin
9CFX 2.7 Å, Cryo-EM structure of myosin-1c bound to F-actin in the Rigor state
9CFU 2.8 Å, Cryo-EM structure of myosin-1c bound to F-actin in the ADP-A state
9CFW 3.0 Å, Cryo-EM structure of myosin-1c bound to F-actin in the ADP-B state
8PB1 3.5 Å, Cryo-EM structure of a pre-dimerized murine IL-12 complete extracellular signaling…

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