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- PDB-9syu: shutdown state non-muscle myosin 2A heads region -

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Basic information

Entry
Database: PDB / ID: 9syu
Titleshutdown state non-muscle myosin 2A heads region
Components
  • (Isoform 1 of ...) x 2
  • Myosin regulatory light polypeptide 9
KeywordsMOTOR PROTEIN / Myosin / coiled coil
Function / homology
Function and homology information


Ephrin signaling / negative regulation of actin filament severing / regulation of plasma membrane repair / blood vessel endothelial cell migration / cytokinetic process / myosin II filament / cortical granule exocytosis / actomyosin contractile ring / positive regulation of protein processing in phagocytic vesicle / cortical granule ...Ephrin signaling / negative regulation of actin filament severing / regulation of plasma membrane repair / blood vessel endothelial cell migration / cytokinetic process / myosin II filament / cortical granule exocytosis / actomyosin contractile ring / positive regulation of protein processing in phagocytic vesicle / cortical granule / myofibril assembly / uropod / regulated exocytosis / myosin II binding / muscle myosin complex / actin filament-based movement / platelet formation / lysosome localization / plasma membrane repair / actomyosin / myosin filament / RHO GTPases Activate ROCKs / actomyosin structure organization / RHO GTPases activate CIT / Sema4D induced cell migration and growth-cone collapse / myosin II complex / Sensory processing of sound by outer hair cells of the cochlea / CD163 mediating an anti-inflammatory response / leukocyte migration / phagocytosis, engulfment / Sensory processing of sound by inner hair cells of the cochlea / structural constituent of muscle / EPHA-mediated growth cone collapse / microfilament motor activity / myosin heavy chain binding / membrane protein ectodomain proteolysis / cell leading edge / cleavage furrow / monocyte differentiation / cytoskeletal motor activity / RHO GTPases activate PAKs / brush border / immunological synapse / RHO GTPases activate PKNs / ruffle / stress fiber / protein-membrane adaptor activity / integrin-mediated signaling pathway / FCGR3A-mediated phagocytosis / Translocation of SLC2A4 (GLUT4) to the plasma membrane / adherens junction / neuromuscular junction / ADP binding / Regulation of actin dynamics for phagocytic cup formation / platelet aggregation / integrin binding / spindle / cytoplasmic side of plasma membrane / actin filament binding / Signaling by ALK fusions and activated point mutants / actin cytoskeleton / regulation of cell shape / protein transport / virus receptor activity / actin cytoskeleton organization / actin binding / angiogenesis / cell cortex / calmodulin binding / cadherin binding / protein domain specific binding / focal adhesion / calcium ion binding / symbiont entry into host cell / Golgi apparatus / magnesium ion binding / cell surface / protein homodimerization activity / protein-containing complex / RNA binding / extracellular exosome / ATP binding / membrane / identical protein binding / nucleus / plasma membrane / cytosol / cytoplasm
Similarity search - Function
DJBP, EF-hand domain / EF-hand domain / : / RGS domain superfamily / Myosin tail / Myosin tail / Myosin N-terminal SH3-like domain / Myosin S1 fragment, N-terminal / Myosin, N-terminal, SH3-like / Myosin N-terminal SH3-like domain profile. ...DJBP, EF-hand domain / EF-hand domain / : / RGS domain superfamily / Myosin tail / Myosin tail / Myosin N-terminal SH3-like domain / Myosin S1 fragment, N-terminal / Myosin, N-terminal, SH3-like / Myosin N-terminal SH3-like domain profile. / Short calmodulin-binding motif containing conserved Ile and Gln residues. / IQ motif, EF-hand binding site / Myosin motor domain profile. / Myosin head, motor domain / Myosin head (motor domain) / Myosin. Large ATPases. / IQ motif profile. / Kinesin motor domain superfamily / : / EF-hand domain pair / EF-hand, calcium binding motif / EF-Hand 1, calcium-binding site / EF-hand calcium-binding domain. / EF-hand calcium-binding domain profile. / EF-hand domain / EF-hand domain pair / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
ADENOSINE-5'-DIPHOSPHATE / PHOSPHATE ION / Myosin light polypeptide 6 / Myosin-9 / Myosin regulatory light polypeptide 9
Similarity search - Component
Biological speciesHomo sapiens (human)
Gallus gallus (chicken)
Bos taurus (domestic cattle)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.98 Å
AuthorsPeckham, M. / Carrington, G.
Funding support United Kingdom, 1items
OrganizationGrant numberCountry
Wellcome TrustRGIMCB124415 United Kingdom
CitationJournal: Sci Adv / Year: 2026
Title: Cryo-EM structure of shutdown human nonmuscle myosin 2A.
Authors: David Casas-Mao / Glenn Carrington / Michelle Peckham /
Abstract: Determining the high-resolution structure of the widely expressed nonmuscle myosin 2A (NM2A), in its dephosphorylated shutdown state, is important in understanding its regulation and disease roles. ...Determining the high-resolution structure of the widely expressed nonmuscle myosin 2A (NM2A), in its dephosphorylated shutdown state, is important in understanding its regulation and disease roles. In shutdown molecules, the coiled-coil tail wraps around the myosin heads, preventing them from forming filaments and binding to actin. We have solved the shutdown structure of NM2A to a global resolution of 3.0 angstroms in the head region and 6.3 angstroms for the whole molecule. This reveals specific ionic interactions that explain why the path of the coiled coil and the shutdown mechanism for NM2A differ from those of β-cardiac myosin and provides key insight into how specific mutations likely destabilize the shutdown state, leading to disease.
History
DepositionOct 14, 2025Deposition site: PDBE / Processing site: PDBE
Revision 1.0Oct 22, 2025Provider: repository / Type: Initial release
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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Isoform 1 of Myosin-9
B: Isoform 1 of Myosin-9
C: Isoform 1 of Myosin light polypeptide 6
D: Isoform 1 of Myosin light polypeptide 6
E: Myosin regulatory light polypeptide 9
F: Myosin regulatory light polypeptide 9
G: Isoform 1 of Myosin-9
H: Isoform 1 of Myosin-9
hetero molecules


Theoretical massNumber of molelcules
Total (without water)982,48616
Polymers981,3448
Non-polymers1,1428
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1

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Components

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Isoform 1 of ... , 2 types, 6 molecules ABGHCD

#1: Protein
Isoform 1 of Myosin-9 / Cellular myosin heavy chain / type A / Myosin heavy chain 9 / Myosin heavy chain / non-muscle IIa / ...Cellular myosin heavy chain / type A / Myosin heavy chain 9 / Myosin heavy chain / non-muscle IIa / Non-muscle myosin heavy chain A / NMMHC-A / Non-muscle myosin heavy chain IIa / NMMHC II-a / NMMHC-IIA


Mass: 226888.781 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: MYH9 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: P35579
#2: Protein Isoform 1 of Myosin light polypeptide 6 / G2 catalytic / LC17-GI / LC17-NM / Myosin light chain alkali smooth-muscle/non-muscle isoforms


Mass: 17004.221 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Gallus gallus (chicken) / Gene: MYL6 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: P02607

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Protein , 1 types, 2 molecules EF

#3: Protein Myosin regulatory light polypeptide 9 / Myosin regulatory light chain 2 / smooth muscle isoform / Myosin regulatory light chain 9


Mass: 19890.211 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bos taurus (domestic cattle) / Gene: MYL9, MYRL2 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: Q5E9E2

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Non-polymers , 3 types, 8 molecules

#4: Chemical ChemComp-ADP / ADENOSINE-5'-DIPHOSPHATE


Mass: 427.201 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H15N5O10P2 / Feature type: SUBJECT OF INVESTIGATION / Comment: ADP, energy-carrying molecule*YM
#5: Chemical ChemComp-PO4 / PHOSPHATE ION


Mass: 94.971 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: PO4 / Feature type: SUBJECT OF INVESTIGATION
#6: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Mg / Feature type: SUBJECT OF INVESTIGATION

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Details

Has ligand of interestY
Has protein modificationN

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: NM2A complex with essential and regulatory light chains in the shutdown state
Type: COMPLEX / Entity ID: #1-#3 / Source: RECOMBINANT
Molecular weightValue: 0.527 MDa / Experimental value: NO
Source (natural)Organism: Homo sapiens (human)
Source (recombinant)Organism: Spodoptera frugiperda (fall armyworm)
Buffer solutionpH: 7.2
Details: 140 mM KCl, 10 mM MOPS pH 7.2, 0.1 mM EGTA, 2 mM MgCl2, 1 mM ATP. 1 mM Bissulfosuccinimidyl suberate
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportGrid type: UltrAuFoil
VitrificationCryogen name: ETHANE / Humidity: 90 %

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal magnification: 96000 X / Nominal defocus max: 3000 nm / Nominal defocus min: 900 nm / Cs: 2.7 mm
Specimen holderSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER
Image recordingAverage exposure time: 3.42 sec. / Electron dose: 36.94 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k) / Num. of grids imaged: 2 / Num. of real images: 27549

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Processing

EM software
IDNameVersionCategory
1cryoSPARCv4.7.0particle selection
2EPU3.3image acquisition
4cryoSPARCCTF correction
10cryoSPARCinitial Euler assignment
11cryoSPARCfinal Euler assignment
13cryoSPARC3D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 2.98 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 186265 / Num. of class averages: 1 / Symmetry type: POINT

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