7PLZ: Actomyosin-V complex in the rigor state

Cryo-EM structure of the actomyosin-V complex in the rigor state (central 3er/2er, young JASP-stabilized F-actin). Determined by electron microscopy at 3.2 Å resolution. Released 22 Dec 2021.

Method: Electron microscopy
Resolution: 3.2 Å
Organisms: Gallus gallus, Oryctolagus cuniculus, Homo sapiens
Chains: 7
Atoms: 23,278
Mol. weight: 347.01 kDa
Ligands: 9UE, MG, PO4, ADP
Released: 22 Dec 2021

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

Secondary structure: helices and β-sheets

7PLZ contains 167 α-helices and 124 β-strands across 7 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, 28 β-strands

Element	Residues	Length	Sheet
β-strand	12-16	5	1
β-strand	22-27	6	1
β-strand	37-41	5	1
β-strand	47-51	5	1
α-helix	60-61	2
β-strand	62	1	1
α-helix	63-65	3
β-strand	73	1	2
α-helix	74-76	3
α-helix	82-91	10
α-helix	92-96	5
β-strand	100-103	4	2
β-strand	106-110	5	2
α-helix	121-127	7
α-helix	139-152	14
β-strand	157-162	6	2
α-helix	165-167	3
α-helix	169-184	16
α-helix	193-207	15
β-strand	208-209	2	3
β-strand	210	1	4
β-strand	217-218	2	3
β-strand	221-228	8	2
β-strand	234-242	9	2
α-helix	247-250	4
β-strand	257	1	4
α-helix	260-267	8
α-helix	273-277	5
α-helix	286-289	4
α-helix	296	1
α-helix	301-314	14
α-helix	319-336	18
β-strand	341-344	4	5
β-strand	347-349	3	5
α-helix	350-351	2
α-helix	355-364	10
α-helix	368-374	7
β-strand	377-381	5	6
β-strand	386-390	5	6
α-helix	393-423	31
α-helix	428-429	2
β-strand	431-437	7	2
α-helix	449-479	31
α-helix	484-486	3
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	564-568	5
α-helix	574-581	8
α-helix	588-592	5
α-helix	631-633	3
α-helix	636-652	17
β-strand	655	1	2
β-strand	658-662	5	2
α-helix	675-684	10
α-helix	687-695	9
β-strand	700-703	4	8
α-helix	704-711	8
α-helix	724-735	12
α-helix	739-741	3
β-strand	742-744	3	8
β-strand	748-751	4	8
α-helix	755-791	37

Chain B: 10 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	6-19	14
β-strand	26-28	3	14
α-helix	29-38	10
α-helix	45-52	8
α-helix	57-62	6
β-strand	64-66	3	14
α-helix	67-78	12
α-helix	87-95	9
β-strand	105	1	15
α-helix	106-115	10
α-helix	119-121	3
α-helix	122-129	8
β-strand	133	1	16
β-strand	138	1	15
β-strand	139	1	16
α-helix	141-149	9

Chain C: 24 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	6-7	2
β-strand	8-11	4	9
β-strand	17-21	5	9
β-strand	29-31	3	9
β-strand	35-38	4	10
β-strand	53-54	2	10
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	10
β-strand	71-72	2	11
β-strand	75-76	2	11
α-helix	79-87	9
α-helix	88-94	7
α-helix	98-100	3
β-strand	103-107	5	9
α-helix	113-126	14
β-strand	131-136	6	9
α-helix	137-145	9
β-strand	149-155	7	12
β-strand	160-166	7	12
β-strand	169-170	2	12
α-helix	172-174	3
β-strand	176-178	3	12
α-helix	182-193	12
α-helix	194-196	3
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	13
β-strand	247-250	4	13
α-helix	253-259	7
α-helix	264-266	3
α-helix	274-283	10
α-helix	290-295	6
β-strand	297-300	4	12
α-helix	302-304	3
α-helix	309-320	12
β-strand	330	1	12
α-helix	333-336	4
α-helix	338-348	11
α-helix	351-354	4
β-strand	357-358	2	9
α-helix	359-365	7
α-helix	369-373	5

Chain D: 37 helices, 28 β-strands

Element	Residues	Length	Sheet
β-strand	11-16	6	17
β-strand	22-27	6	17
β-strand	37-41	5	17
β-strand	47-51	5	17
α-helix	60-61	2
β-strand	62	1	17
α-helix	63-65	3
β-strand	73	1	18
α-helix	74-76	3
α-helix	82-96	15
β-strand	100-103	4	18
β-strand	106-110	5	18
α-helix	121-127	7
α-helix	139-152	14
β-strand	157-162	6	18
α-helix	165-167	3
α-helix	169-184	16
α-helix	193-207	15
β-strand	208-209	2	19
β-strand	210	1	20
β-strand	217-218	2	19
β-strand	221-228	8	18
β-strand	234-242	9	18
α-helix	247-250	4
β-strand	257	1	20
α-helix	260-267	8
α-helix	273-277	5
α-helix	286-289	4
α-helix	296	1
α-helix	301-314	14
α-helix	319-336	18
β-strand	341-344	4	21
β-strand	347-349	3	21
α-helix	350-351	2
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	431-438	8	18
α-helix	449-479	31
α-helix	484-486	3
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	564-568	5
α-helix	574-581	8
α-helix	588-592	5
α-helix	631-633	3
α-helix	636-652	17
β-strand	655	1	18
β-strand	658-662	5	18
α-helix	675-684	10
α-helix	687-696	10
β-strand	700-703	4	24
α-helix	704-711	8
α-helix	724-735	12
α-helix	739-741	3
β-strand	742-744	3	24
β-strand	748-751	4	24
α-helix	755-791	37

Chain E: 10 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	6-19	14
β-strand	26-28	3	30
α-helix	29-38	10
α-helix	45-52	8
α-helix	57-62	6
β-strand	64-66	3	30
α-helix	67-78	12
α-helix	87-95	9
β-strand	103-105	3	31
α-helix	106-115	10
α-helix	119-121	3
α-helix	122-129	8
β-strand	138-140	3	31
α-helix	141-149	9

Chain F: 24 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	6-7	2
β-strand	8-11	4	25
β-strand	17-21	5	25
β-strand	29-31	3	25
β-strand	35-38	4	26
β-strand	53-54	2	26
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	26
β-strand	71-72	2	27
β-strand	75-76	2	27
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	25
α-helix	113-126	14
β-strand	131-136	6	25
α-helix	137-145	9
β-strand	149-155	7	28
β-strand	160-166	7	28
β-strand	169-170	2	28
α-helix	172-174	3
β-strand	176-178	3	28
α-helix	182-193	12
α-helix	194-196	3
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	29
β-strand	247-250	4	29
α-helix	253-259	7
α-helix	264-266	3
α-helix	274-283	10
α-helix	290-295	6
β-strand	297-300	4	28
α-helix	302-304	3
α-helix	309-320	12
β-strand	330	1	28
α-helix	333-336	4
α-helix	338-348	11
α-helix	351-354	4
β-strand	357-358	2	25
α-helix	359-365	7
α-helix	369-373	5

Chain G: 24 helices, 20 β-strands

Element	Residues	Length	Sheet
α-helix	6-7	2
β-strand	8-11	4	32
β-strand	16-21	6	32
β-strand	29-32	4	32
β-strand	35-38	4	33
β-strand	42	1	28
β-strand	53-54	2	33
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	33
β-strand	71-72	2	34
β-strand	75-76	2	34
α-helix	79-87	9
α-helix	88-94	7
α-helix	98-100	3
β-strand	103-107	5	32
α-helix	113-121	9
α-helix	122-126	5
β-strand	131-136	6	32
α-helix	137-145	9
β-strand	149-155	7	35
β-strand	160-166	7	35
β-strand	169-170	2	35
α-helix	172-174	3
β-strand	176-178	3	35
α-helix	182-193	12
α-helix	194-196	3
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	36
β-strand	247-250	4	36
α-helix	253-259	7
α-helix	264-266	3
α-helix	274-283	10
α-helix	290-295	6
β-strand	297-300	4	35
α-helix	302-304	3
α-helix	309-320	12
β-strand	330	1	35
α-helix	338-348	11
α-helix	351-354	4
β-strand	357-358	2	32
α-helix	359-365	7
α-helix	369-373	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Unconventional myosin-Va	A, D	protein	792	Gallus gallus	Q02440 (AlphaFold model)
Actin, alpha skeletal muscle	C, F, G	protein	377	Oryctolagus cuniculus	P68135 (AlphaFold model)
Myosin light chain 6B	B, E	protein	151	Homo sapiens	P14649 (AlphaFold model)

Sequence of entity 1 (A, D), FASTA

>7PLZ_1 Unconventional myosin-Va (chains A, D)
MAASELYTKYARVWIPDPEEVWKSAELLKDYKPGDKVLQLRLEEGKDLEYCLDPKTKELP
PLRNPDILVGENDLTALSYLHEPAVLHNLKVRFIDSKLIYTYCGIVLVAINPYEQLPIYG
EDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGESGAGKTVSAKYAMRYF
ATVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMR
TYLLEKSRVVFQAEEERNYHIFYQLCASAALPEFKTLRLGNANYFHYTKQGGSPVIDGID
DAKEMVNTRQACTLLGISDSYQMGIFRILAGILHLGNVEFASRDSDSCAIPPKHDPLTIF
CDLMGVDYEEMAHWLCHRKLATATETYIKPISKLHAINARDALAKHIYANLFNWIVDHVN
KALHSTVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKE
QIPWTLIDFYDNQPCINLIEAKMGVLDLLDEECKMPKGSDDTWAQKLYNTHLNKCALFEK
PRLSNKAFIIKHFADKVEYQCEGFLEKNKDTVYEEQIKVLKSSKKFKLLPELFQDEEKAI
SPTSATPSGRVPLSRTPVKPAKARPGQTSKEHKKTVGHQFRNSLHLLMETLNATTPHYVR
CIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQKDV
LSDRKQTCKNVLEKLILDKDKYQFGKTKIFFRAGQVAYLEKIRADKLRAACIRIQKTIRG
WLMRKKYMRMRR

Sequence of entity 2 (C, F, G), FASTA

>7PLZ_2 Actin, alpha skeletal muscle (chains C, F, G)
MCDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEA
QSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREK
MTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRL
DLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEK
SYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNV
MSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWIT
KQEYDEAGPSIVHRKCF

Sequence of entity 3 (B, E), FASTA

>7PLZ_3 Myosin light chain 6B (chains B, E)
MIEFNKDQLEEFKEAFELFDRVGDGKILYSQCGDVMRALGQNPTNAEVLKVLGNPKSDEL
KSRRVDFETFLPMLQAVAKNRGQGTYEDYLEGFRVFDKEGNGKVMGAELRHVLTTLGEKM
TEEEVETVLAGHEDSNGCINYEAFLKHILSV

Ligands and cofactors

ID	Name	Formula	Copies
9UE	Jasplakinolide	C36 H45 Br N4 O6	3
MG	Magnesium ion	Mg	3
PO4	Phosphate ion	O4 P	3
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	3

Primary citation

High-resolution structures of the actomyosin-V complex in three nucleotide states provide insights into the force generation mechanism. Pospich, S., Sweeney, H.L., Houdusse, A. et al. Elife (2021) 10. DOI 10.7554/eLife.73724 · PubMed

Other PDB entries of the same protein (UniProt Q02440 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1W7J 2.0 Å, Crystal Structure Of Myosin V Motor With Essential Light Chain + ADP-BeFx - Near Rigor
1OE9 2.05 Å, Crystal structure of Myosin V motor with essential light chain-nucleotide-free
1W8J 2.7 Å, Crystal Structure Of Myosin V Motor Domain - Nucleotide-Free
7PMD 2.9 Å, Cryo-EM structure of the actomyosin-V complex in the post-rigor transition state…
7PME 2.9 Å, Cryo-EM structure of the actomyosin-V complex in the post-rigor transition state…
1W7I 3.0 Å, Crystal Structure Of Myosin V Motor Without nucleotide soaked in 10 mM MgADP
7PM6 3.0 Å, Cryo-EM structure of the actomyosin-V complex in the strong-ADP state (central 3er/2er)
7PM5 3.1 Å, Cryo-EM structure of the actomyosin-V complex in the strong-ADP state (central 1er)
7PLU 3.2 Å, Cryo-EM structure of the actomyosin-V complex in the rigor state (central 3er/2er)
7PLY 3.2 Å, Cryo-EM structure of the actomyosin-V complex in the rigor state (central 1er, young…
7PLT 3.3 Å, Cryo-EM structure of the actomyosin-V complex in the rigor state (central 1er)
7PMG 3.3 Å, Cryo-EM structure of the actomyosin-V complex in the post-rigor transition state…

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