7R91: Rigor state wild type myosin-15-F-actin complex

cryo-EM structure of the rigor state wild type myosin-15-F-actin complex. Determined by electron microscopy at 2.83 Å resolution. Released 28 Jul 2021.

Method
Electron microscopy
Resolution
2.83 Å
Organisms
Gallus gallus, Mus musculus
Chains
4
Atoms
14,320
Mol. weight
204.43 kDa
Ligands
MG, ADP
Released
28 Jul 2021

Explore 7R91 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7R91 contains 103 α-helices and 78 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, 20 β-strands

ElementResiduesLengthSheet
β-strand8-1251
β-strand16-2161
β-strand29-3241
β-strand35-3842
β-strand41-4223
β-strand53-5422
α-helix56-605
β-strand65-6842
β-strand71-7224
β-strand75-7624
α-helix79-879
α-helix88-936
α-helix98-1003
β-strand103-10751
α-helix113-12513
β-strand131-13661
α-helix137-1459
β-strand150-15565
β-strand160-16675
β-strand169-17025
α-helix172-1743
β-strand176-17835
α-helix182-19211
α-helix193-1964
α-helix203-21614
α-helix223-23210
β-strand238-24146
β-strand247-25046
α-helix253-2564
α-helix258-2614
α-helix264-2674
α-helix271-2733
α-helix274-28310
α-helix290-2945
β-strand297-30045
α-helix303-3053
α-helix309-32012
β-strand329-33025
α-helix335-3373
α-helix338-34710
α-helix351-3544
β-strand357-35821
α-helix359-3657
α-helix366-3683
α-helix369-3735
Chains B and C: 25 helices, 19 β-strands
ElementResiduesLengthSheet
β-strand8-1257
β-strand16-2167
β-strand29-3247
β-strand35-3848
β-strand53-5428
α-helix56-605
β-strand65-6848
β-strand71-7229
β-strand75-7629
α-helix79-879
α-helix88-936
α-helix98-1003
β-strand103-10757
α-helix113-12513
β-strand131-13667
α-helix137-1459
β-strand150-15563
β-strand160-16673
β-strand169-17023
α-helix172-1743
β-strand176-17833
α-helix182-19211
α-helix193-1964
α-helix203-21614
α-helix223-23210
β-strand238-241410
β-strand247-250410
α-helix253-2564
α-helix258-2614
α-helix264-2674
α-helix271-2733
α-helix274-28310
α-helix290-2945
β-strand297-30043
α-helix303-3053
α-helix309-32012
β-strand329-33023
α-helix335-3373
α-helix338-34710
α-helix351-3544
β-strand357-35827
α-helix359-3657
α-helix366-3683
α-helix369-3735
Chain D: 28 helices, 20 β-strands
ElementResiduesLengthSheet
β-strand1210116
α-helix1211-12133
α-helix1219-123113
β-strand1237-1239316
β-strand1242-1246516
α-helix1257-12626
α-helix1275-128915
β-strand1293-1299716
α-helix1305-131915
α-helix1326-13327
α-helix1335-13428
β-strand1343-1344217
β-strand1352-1353217
β-strand1356-1364916
β-strand1367-13761016
β-strand1393117
α-helix1394-14029
α-helix1405-14117
α-helix1435-144814
α-helix1453-146917
β-strand1474-1478518
β-strand1483-1487518
α-helix1491-150010
α-helix1504-15129
β-strand1513-1517519
β-strand1522-1526519
α-helix1529-155830
β-strand1566-1572716
α-helix1584-161431
α-helix1628-16358
α-helix1641-16488
α-helix1656-166712
β-strand1673-1674220
β-strand1682-1687620
β-strand1690-1695620
β-strand1704121
α-helix1709-17168
α-helix1721-173313
β-strand1753121
α-helix1754-176714
β-strand1775-1780616
α-helix1793-180311
α-helix1806-18127
α-helix1822-18287
α-helix1829-18313
α-helix1844-18529
α-helix1858-18603
α-helix1874-188815

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Actin, alpha skeletal muscle, intermediate formA, B, Cprotein373Gallus gallusP68139 (AlphaFold model)
Isoform 3 of Unconventional myosin-XVDprotein685Mus musculusQ9QZZ4 (AlphaFold model)
Sequence of entity 1 (A, B, C), FASTA
>7R91_1 Actin, alpha skeletal muscle, intermediate form (chains A, B, C)
DETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKR
GILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMTQI
MFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLAG
RDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYEL
PDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMSGG
TTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQEY
DEAGPSIVHRKCF
Sequence of entity 2 (D), FASTA
>7R91_2 Isoform 3 of Unconventional myosin-XV (chains D)
EDGVEDMTQLEDLQETTVLANLKTRFERNLIYTYIGSILVSVNPYRMFAIYGPEQVQQYS
GRALGENPPHLFAIANLAFAKMLDAKQNQCVIISGESGSGKTEATKLILRCLAAMNQRRD
VMQQIKILEATPLLEAFGNAKTVRNDNSSRFGKFVEIFLEGGVICGAITSQYLLEKSRIV
FQAKNERNYHIFYELLAGLPAQLRQAFSLQEAETYYYLNQGGNCEIAGKSDADDFRRLLA
AMEVLGFTSEDQDSIFRILASILHLGNVYFEKHETDAQEVASVVSAREIQAVAELLQVSP
EGLQKAITFKVTETIREKIFTPLTVESAVDARDAIAKVLYALLFGWLITRVNALVSPKQD
TLSIAILDIYGFEDLSFNSFEQLCINYANENLQYLFNKIVFQEEQEEYIREQMDWREIAF
ADNQPCINLISLKPYGILRILDDQCCFPQATDHTFLQKCHYHHGANPLYSKPKMPLPEFT
IKHYAGKVTYQVHKFLDKNHDQVRQDVLDLFVHSRTRVVAHLFSSHAAQTAPPRLGKSSS
ITRLYKAHTVAAKFQQSLLDLVEKMERCNPLFVRCLKPNHKKEPGLFEPDVMMAQLRYSG
VLETVRIRKEGFPVRLPFQVFIDRYRCLVALKLNVPADGDMCVSLLSRLCTVTPDMYRVG
ISKLFLKEHLHQLLESMRERVQNRA

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg3
ADPAdenosine-5'-diphosphateC10 H15 N5 O10 P23

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:

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