7YV9: Full-length Myosin Va in the autoinhibited state

Cryo-EM structure of full-length Myosin Va in the autoinhibited state. Determined by electron microscopy at 4.78 Å resolution. Released 21 Dec 2022.

Method: Electron microscopy
Resolution: 4.78 Å
Organism: Mus musculus
Chains: 16
Atoms: 37,510
Mol. weight: 1052.81 kDa
Released: 21 Dec 2022

Explore 7YV9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7YV9 contains 227 α-helices and 99 β-strands across 16 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: 40 helices, 27 β-strands

Element	Residues	Length	Sheet
β-strand	11-16	6	1
β-strand	22-27	6	1
α-helix	30-31	2
β-strand	37	1	2
β-strand	40-42	3	1
β-strand	47-48	2	1
α-helix	50	1
β-strand	51	1	2
α-helix	52	1
α-helix	59-61	3
β-strand	62	1	1
α-helix	63-65	3
α-helix	74-76	3
α-helix	82-90	9
α-helix	91-95	5
β-strand	101-103	3	3
β-strand	106-110	5	3
α-helix	117-119	3
α-helix	121-127	7
α-helix	136-137	2
α-helix	139-152	14
β-strand	157-163	7	3
α-helix	169-184	16
α-helix	187-207	21
β-strand	208-209	2	4
β-strand	217-218	2	4
β-strand	221-228	8	3
β-strand	234-242	9	3
α-helix	247-250	4
β-strand	259	1	4
α-helix	260-267	8
α-helix	272-277	6
α-helix	282-284	3
α-helix	301-314	14
α-helix	319-335	17
β-strand	341	1	5
β-strand	349	1	5
α-helix	350-351	2
α-helix	355-364	10
α-helix	368-376	9
β-strand	377-381	5	6
β-strand	386-390	5	6
α-helix	391-392	2
α-helix	393-423	31
β-strand	431-437	7	3
α-helix	449-479	31
α-helix	493-500	8
α-helix	505-514	10
α-helix	520-531	12
β-strand	538-539	2	7
β-strand	547-551	5	7
β-strand	556-560	5	7
α-helix	562-568	7
α-helix	574-581	8
α-helix	588-592	5
α-helix	629-632	4
α-helix	635-651	17
β-strand	654-661	8	3
α-helix	674-684	11
α-helix	686-695	10
β-strand	699-702	4	8
α-helix	703-709	7
α-helix	723-734	12
β-strand	741-742	2	8
β-strand	747-750	4	8
α-helix	752-907	156
α-helix	915-1099	185

Chain B: 8 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	7-20	14
β-strand	29	1	9
α-helix	30-39	10
α-helix	46-59	14
β-strand	63	1	9
α-helix	66-78	13
α-helix	83-93	11
β-strand	100-101	2	10
α-helix	103-111	9
α-helix	119-128	10
β-strand	137-138	2	10
α-helix	139-147	9

Chain C: 11 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	4-6	3
α-helix	7-20	14
β-strand	28	1	11
α-helix	30-39	10
α-helix	46-56	11
β-strand	64	1	11
α-helix	66-75	10
α-helix	83-93	11
β-strand	100-102	3	12
α-helix	103-112	10
α-helix	116-118	3
α-helix	119-128	10
α-helix	130-131	2
β-strand	136-138	3	12
α-helix	139-148	10

Chain D: 10 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	4-6	3
α-helix	7-20	14
β-strand	28-29	2	13
α-helix	30-39	10
α-helix	46-59	14
β-strand	63-64	2	13
α-helix	66-77	12
α-helix	83-93	11
β-strand	100-102	3	14
α-helix	103-112	10
α-helix	116-118	3
α-helix	119-128	10
β-strand	136-138	3	14
α-helix	140-148	9

Chain E: 8 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	7-20	14
β-strand	27-29	3	15
α-helix	30-39	10
α-helix	46-59	14
β-strand	63-65	3	15
α-helix	66-78	13
α-helix	83-92	10
β-strand	100-101	2	16
α-helix	103-112	10
α-helix	119-129	11
β-strand	137-138	2	16
α-helix	140-148	9

Chain F: 8 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	7-20	14
α-helix	30-40	11
α-helix	46-59	14
α-helix	66-78	13
α-helix	83-93	11
β-strand	100-102	3	17
α-helix	103-112	10
α-helix	119-129	11
β-strand	136-138	3	17
α-helix	139-148	10

Chain G: 10 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	7-20	14
α-helix	30-38	9
α-helix	46-56	11
α-helix	66-77	12
α-helix	83-93	11
β-strand	101	1	18
α-helix	103-111	9
α-helix	119-129	11
α-helix	136	1
β-strand	137	1	18
α-helix	138	1
α-helix	139-148	10

Chain H: 36 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	11-16	6	19
β-strand	22-27	6	19
α-helix	30-31	2
β-strand	37-42	6	19
β-strand	47-51	5	19
α-helix	58-59	2
α-helix	61	1
β-strand	62	1	19
β-strand	73	1	20
α-helix	82-91	10
α-helix	92-96	5
β-strand	100-103	4	20
β-strand	106-110	5	20
α-helix	117-119	3
α-helix	121-127	7
α-helix	136-137	2
α-helix	139-153	15
β-strand	157-161	5	20
α-helix	169-184	16
α-helix	187-207	21
β-strand	209	1	21
β-strand	217	1	21
β-strand	221-228	8	20
β-strand	234-242	9	20
β-strand	259	1	21
α-helix	260-267	8
α-helix	272-274	3
α-helix	282-284	3
α-helix	286-289	4
α-helix	301-315	15
α-helix	319-334	16
α-helix	355-364	10
α-helix	368-374	7
β-strand	377-381	5	22
β-strand	386-390	5	22
α-helix	393-423	31
α-helix	428-429	2
β-strand	431-437	7	20
α-helix	439-442	4
α-helix	449-479	31
α-helix	493-500	8
α-helix	505-514	10
α-helix	520-531	12
β-strand	538-539	2	23
β-strand	547-551	5	23
β-strand	556-560	5	23
α-helix	561-568	8
α-helix	574-580	7
α-helix	587-592	6
α-helix	635-652	18
β-strand	654-661	8	20
α-helix	674-684	11
α-helix	686-695	10
β-strand	699-702	4	24
α-helix	703-709	7
α-helix	723-734	12
β-strand	741-742	2	24
β-strand	747-750	4	24
α-helix	752-907	156
α-helix	916-1101	186

8 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
Unconventional myosin-Va	A, H, X, Y	protein	1828	Mus musculus	Q99104 (AlphaFold model)
Calmodulin-1	B, C, D, E, F, G, I, J, K, L, M, N	protein	149	Mus musculus	P0DP26 (AlphaFold model)

Sequence of entity 1 (A, H, X, Y), FASTA

>7YV9_1 Unconventional myosin-Va (chains A, H, X, Y)
MAASELYTKFARVWIPDPEEVWKSAELLKDYKPGDKVLLLHLEEGKDLEYRLDPKTGELP
HLRNPDILVGENDLTALSYLHEPAVLHNLRVRFIDSKLIYTYCGIVLVAINPYEQLPIYG
EDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGESGAGKTVSAKYAMRYF
ATVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMR
TYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADSFHYTKQGGSPMIEGVD
DAKEMAHTRQACTLLGISESYQMGIFRILAGILHLGNVGFASRDSDSCTIPPKHEPLTIF
CDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDHVN
QALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKE
QIPWTLIDFYDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEK
PRMSNKAFIIKHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAIS
PTSATSSGRTPLTRVPVKPTKGRPGQTAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRC
IKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQKDVL
GDRKQTCKNVLEKLILDKDKYQFGKTKIFFRAGQVAYLEKLRADKLRAACIRIQKTIRGW
LLRKRYLCMQRAAITVQRYVRGYQARCYAKFLRRTKAATTIQKYWRMYVVRRRYKIRRAA
TIVIQSYLRGYLTRNRYRKILREYKAVIIQKRVRGWLARTHYKRTMKAIVYLQCCFRRMM
AKRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLMEKLTNLEGVYNSE
TEKLRNDVERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKSIEERADKYKQET
DQLVSNLKEENTLLKQEKETLNHRIVEQAKEMTETMERKLVEETKQLELDLNDERLRYQN
LLNEFSRLEERYDDLKEEMTLMLNVPKPGHKRTDSTHSSNESEYTFSSEFAETEDIAPRT
EEPIEKKVPLDMSLFLKLQKRVTELEQEKQLMQDELDRKEEQVFRSKAKEEERPQIRGAE
LEYESLKRQELESENKKLKNELNELRKALSEKSAPEVTAPGAPAYRVLMEQLTSVSEELD
VRKEEVLILRSQLVSQKEAIQPKDDKNTMTDSTILLEDVQKMKDKGEIAQAYIGLKETNR
LLESQLQSQKRSHENEAEALRGEIQSLKEENNRQQQLLAQNLQLPPEARIEASLQHEITR
LTNENLDLMEQLEKQDKTVRKLKKQLKVFAKKIGELEVGQMENISPGQIIDEPIRPVNIP
RKEKDFQGMLEYKREDEQKLVKNLILELKPRGVAVNLIPGLPAYILFMCVRHADYLNDDQ
KVRSLLTSTINSIKKVLKKRGDDFETVSFWLSNTCRFLHCLKQYSGEEGFMKHNTSRQNE
HCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPMIVSGMLEHETIQGVSGVKPTGLR
KRTSSIADEGTYTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIVGAITLNNLLLR
KDMCSWSKGMQIRYNVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEAI
CSMCNALTTAQIVKVLNLYTPVNEFEERVSVSFIRTIQMRLRDRKDSPQLLMDAKHIFPV
TFPFNPSSLALETIQIPASLGLGFIARV

Sequence of entity 2 (B, C, D, E, F, G, I, J, K, L, M, N), FASTA

>7YV9_2 Calmodulin-1 (chains B, C, D, E, F, G, I, J, K, L, M, N)
MADQLTEEQIAEFKEAFSLFDKDGDGTITTKQLGTVMRSLGQNPTEAELQDMINEVDADG
NGTIDFPQFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAQLRHVMTNLGEKLTDE
EVDEMIREADIDGDGQVNYEQFVQMMTAK

Primary citation

Autoinhibition and activation mechanisms revealed by the triangular-shaped structure of myosin Va. Niu, F., Liu, Y., Sun, K. et al. Sci Adv (2022) 8:eadd4187-eadd4187. DOI 10.1126/sciadv.add4187 · 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
8RBF 4.2 Å, CryoEM structure of the post-powerstroke actomyosin-5a complex
8R9V 4.4 Å, CryoEM structure of the primed actomyosin-5a complex
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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