7RB9: Rigor state Jordan myosin-15-F-actin complex

Cryo-EM structure of the rigor state Jordan myosin-15-F-actin complex. Determined by electron microscopy at 3.76 Å resolution. Released 28 Jul 2021.

Method: Electron microscopy
Resolution: 3.76 Å
Organisms: Gallus gallus, Mus musculus
Chains: 4
Atoms: 14,193
Mol. weight: 204.37 kDa
Ligands: ADP, MG
Released: 28 Jul 2021

Explore 7RB9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7RB9 contains 110 α-helices and 83 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: 25 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	14
β-strand	16-21	6	14
β-strand	29-32	4	14
β-strand	35-38	4	15
β-strand	41-42	2	4
β-strand	53-54	2	15
α-helix	57-60	4
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	80-87	8
α-helix	88-94	7
α-helix	98-100	3
β-strand	103-107	5	14
α-helix	113-125	13
β-strand	131-136	6	14
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	203-216	14
α-helix	223-230	8
β-strand	238-241	4	18
β-strand	247-250	4	18
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-267	4
α-helix	272-273	2
α-helix	274-282	9
α-helix	290-293	4
β-strand	297-298	2	19
β-strand	299-300	2	17
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	19
α-helix	335-337	3
α-helix	338-347	10
α-helix	351-355	5
β-strand	357-358	2	14
α-helix	359-365	7
α-helix	367-369	3
α-helix	370-373	4

Chain B: 25 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	1
β-strand	16-21	6	1
β-strand	29-32	4	1
β-strand	35-38	4	2
β-strand	53-54	2	2
α-helix	57-60	4
α-helix	62-64	3
β-strand	65-68	4	2
β-strand	71-72	2	3
β-strand	75-76	2	3
α-helix	80-87	8
α-helix	88-94	7
α-helix	98-100	3
β-strand	103-107	5	1
α-helix	113-125	13
β-strand	131-136	6	1
α-helix	137-144	8
β-strand	150-155	6	4
β-strand	160-166	7	4
β-strand	169-170	2	4
α-helix	172-174	3
β-strand	176-178	3	4
α-helix	182-193	12
α-helix	203-216	14
α-helix	223-230	8
β-strand	238-241	4	5
β-strand	247-250	4	5
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-267	4
α-helix	272-273	2
α-helix	274-282	9
α-helix	290-293	4
β-strand	297-298	2	6
β-strand	299-300	2	4
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	6
α-helix	335-337	3
α-helix	338-347	10
α-helix	351-355	5
β-strand	357-358	2	1
α-helix	359-365	7
α-helix	367-369	3
α-helix	370-373	4

Chain C: 24 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	20
β-strand	16-21	6	20
β-strand	29-32	4	20
β-strand	35-38	4	21
β-strand	53-54	2	21
α-helix	57-60	4
β-strand	65-68	4	21
β-strand	71-72	2	22
β-strand	75-76	2	22
α-helix	80-87	8
α-helix	88-94	7
α-helix	98-100	3
β-strand	103-107	5	20
α-helix	113-125	13
β-strand	131-136	6	20
α-helix	137-144	8
β-strand	150-155	6	23
β-strand	160-166	7	23
β-strand	169-170	2	23
α-helix	172-174	3
β-strand	176-178	3	23
α-helix	182-193	12
α-helix	203-216	14
α-helix	223-230	8
β-strand	238-241	4	24
β-strand	247-250	4	24
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-267	4
α-helix	272-273	2
α-helix	274-282	9
α-helix	290-293	4
β-strand	297-298	2	25
β-strand	299-300	2	23
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	25
α-helix	335-337	3
α-helix	338-347	10
α-helix	351-355	5
β-strand	357-358	2	20
α-helix	359-365	7
α-helix	367-369	3
α-helix	370-373	4

Chain D: 36 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	1210	1	7
α-helix	1219-1229	11
α-helix	1230-1232	3
β-strand	1237-1238	2	7
β-strand	1243-1246	4	7
α-helix	1253-1255	3
α-helix	1257-1261	5
α-helix	1267-1270	4
α-helix	1272-1273	2
α-helix	1275-1289	15
β-strand	1293-1297	5	7
α-helix	1305-1318	14
α-helix	1322-1324	3
α-helix	1327-1333	7
α-helix	1336-1342	7
β-strand	1343-1344	2	8
β-strand	1352-1353	2	8
β-strand	1355-1364	10	7
β-strand	1367-1378	12	7
α-helix	1380-1383	4
β-strand	1393	1	8
α-helix	1394-1402	9
α-helix	1405-1411	7
α-helix	1429-1432	4
α-helix	1435-1448	14
α-helix	1453-1469	17
β-strand	1474	1	9
β-strand	1478	1	10
β-strand	1483	1	10
β-strand	1487	1	9
α-helix	1491-1500	10
α-helix	1504-1512	9
β-strand	1513-1517	5	11
β-strand	1522-1526	5	11
α-helix	1529-1558	30
α-helix	1560-1561	2
β-strand	1567-1572	6	7
α-helix	1584-1615	32
α-helix	1617-1619	3
α-helix	1628-1635	8
α-helix	1641-1649	9
α-helix	1656-1667	12
β-strand	1673-1674	2	12
β-strand	1682-1687	6	12
β-strand	1690-1695	6	12
α-helix	1699-1702	4
α-helix	1709-1715	7
α-helix	1721-1733	13
α-helix	1754-1769	16
β-strand	1775-1780	6	7
α-helix	1793-1803	11
α-helix	1806-1812	7
β-strand	1819	1	13
α-helix	1822-1828	7
α-helix	1844-1854	11
α-helix	1858-1860	3
β-strand	1869	1	13
α-helix	1874-1886	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Actin, alpha skeletal muscle, intermediate form	A, B, C	protein	373	Gallus gallus	P68139 (AlphaFold model)
Isoform 3 of Unconventional myosin-XV	D	protein	685	Mus musculus	Q9QZZ4 (AlphaFold model)

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

>7RB9_1 Actin, alpha skeletal muscle, intermediate form (chains A, B, C)
DETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKR
GILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMTQI
MFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLAG
RDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYEL
PDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMSGG
TTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQEY
DEAGPSIVHRKCF

Sequence of entity 2 (D), FASTA

>7RB9_2 Isoform 3 of Unconventional myosin-XV (chains D)
EDGVEDMTQLEDLQETTVLANLKTRFERNLIYTYIGSILVSVNPYRMFAIYGPEQVQQYS
GRALGENPPHLFAIANLAFAKMLDAKQNQCVIISGESGSGKTEATKLILRCLAAMNQRRD
VMQQIKILEATPLLEAFGNAKTVRNDNSSRFGKFVEIFLEGGVICGAITSQYLLEKSRIV
FQAKNERNYHIFYELLAGLPAQLRQAFSLQEAETYYYLNQGGNCEIAGKSDADDFRRLLA
AMEVLGFTSEDQDSIFRILASILHLGNVYFEKHETDAQEVASVVSAREIQAVAELLQVSP
EGLQKAITFKVTETIREKIFTPLTVESAVDARDAIAKVLYALLFGWLITRVNALVSPKQD
TLSIAILDIYGFEDLSFNSFEQLCINYANENLQYLFNKIVFQEEQEEYIREQMDWREIAF
ADNQPCINLISLKPYGILRILDGQCCFPQATDHTFLQKCHYHHGANPLYSKPKMPLPEFT
IKHYAGKVTYQVHKFLDKNHDQVRQDVLDLFVHSRTRVVAHLFSSHAAQTAPPRLGKSSS
ITRLYKAHTVAAKFQQSLLDLVEKMERCNPLFVRCLKPNHKKEPGLFEPDVMMAQLRYSG
VLETVRIRKEGFPVRLPFQVFIDRYRCLVALKLNVPADGDMCVSLLSRLCTVTPDMYRVG
ISKLFLKEHLHQLLESMRERVQNRA

Ligands and cofactors

ID	Name	Formula	Copies
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	3
MG	Magnesium ion	Mg	3

Primary citation

Structural basis for tunable control of actin dynamics by myosin-15 in mechanosensory stereocilia. Gong, R., Jiang, F., Moreland, Z.G. et al. Sci Adv (2022) 8:eabl4733-eabl4733. DOI 10.1126/sciadv.abl4733 · PubMed

Other PDB entries of the same protein (UniProt P68139 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7W4Z 1.15 Å, Crystal structure of fragmin domain-1 in complex with actin (AMPPNP-form)
7W50 1.15 Å, Crystal structure of fragmin domain-1 in complex with actin (ADP-Pi-form)
7W51 1.2 Å, Crystal structure of fragmin domain-1 in complex with actin (ADP-form)
9L2N 1.7 Å, Crystal structure of Cytochalasin D bound to a filamentous conformation actin
7W52 2.0 Å, Crystal structure of fragmin domain-1 (15-160) in complex with actin
1MDU 2.2 Å, Crystal structure of the chicken actin trimer complexed with human gelsolin segment 1…
8D13 2.43 Å, Helical ADP-F-actin
8D14 2.51 Å, Helical ADP-Pi-F-actin
7R94 2.6 Å, T-Plastin-F-actin complex
8C4E 2.6 Å, F-actin decorated by SipA426-685
9JW0 2.69 Å, Structure of the N-terminal 3 domains (V1-V3) villin bound to actin
7YNE 2.7 Å, Crystal structure of fragmin domain-1 (1-160) in complex with G-form actin

Browse structure collections

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