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- EMDB-73797: Cryo-EM structure of full-length human NM2B -

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Basic information

Entry
Database: EMDB / ID: EMD-73797
TitleCryo-EM structure of full-length human NM2B
Map dataComposite full-length 10S map
Sample
  • Complex: Nonmuscle myosin 2B
    • Protein or peptide: Myosin-10
    • Protein or peptide: Myosin light polypeptide 6
    • Protein or peptide: Myosin regulatory light chain 12B
  • Ligand: MAGNESIUM ION
  • Ligand: ADENOSINE-5'-DIPHOSPHATE
  • Ligand: PHOSPHATE ION
KeywordsATPase enzyme / MOTOR PROTEIN
Function / homology
Function and homology information


myosin II filament / postsynaptic actin cytoskeleton organization / unconventional myosin complex / actin filament-based movement / actomyosin / myosin filament / RHO GTPases Activate ROCKs / postsynaptic actin cytoskeleton / actomyosin structure organization / RHO GTPases activate CIT ...myosin II filament / postsynaptic actin cytoskeleton organization / unconventional myosin complex / actin filament-based movement / actomyosin / myosin filament / RHO GTPases Activate ROCKs / postsynaptic actin cytoskeleton / actomyosin structure organization / RHO GTPases activate CIT / Sema4D induced cell migration and growth-cone collapse / muscle filament sliding / myosin complex / myosin II complex / structural constituent of muscle / EPHA-mediated growth cone collapse / microfilament motor activity / myosin heavy chain binding / cleavage furrow / myofibril / mitotic cytokinesis / RHO GTPases activate PAKs / cytoskeletal motor activity / brush border / Smooth Muscle Contraction / skeletal muscle tissue development / RHO GTPases activate PKNs / stress fiber / muscle contraction / positive regulation of protein secretion / neuromuscular junction / ADP binding / RNA stem-loop binding / spindle / mRNA 5'-UTR binding / Z disc / cytoplasmic side of plasma membrane / actin filament binding / regulation of cell shape / lamellipodium / growth cone / virus receptor activity / actin binding / midbody / cell cortex / vesicle / dendritic spine / calmodulin binding / cell adhesion / neuronal cell body / calcium ion binding / symbiont entry into host cell / glutamatergic synapse / cell surface / extracellular exosome / ATP binding / membrane / nucleus / cytoplasm / cytosol
Similarity search - Function
DJBP, EF-hand domain / EF-hand domain / : / IQ calmodulin-binding motif / 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 / : / IQ calmodulin-binding motif / 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
Myosin regulatory light chain 12B / Myosin-10 / Myosin light polypeptide 6
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 10.0 Å
AuthorsHeissler SM / Chinthalapudi KC
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R01GM143539 United States
CitationJournal: Nat Commun / Year: 2026
Title: Structural basis of nonmuscle myosin-2 autoinhibition mechanisms.
Authors: Sarah M Heissler / Giovanna Grandinetti / James R Sellers / Krishna Chinthalapudi /
Abstract: Nonmuscle myosin-2 (NM2) is a fundamental actin-based mechanochemical ATPase that regulates cellular architecture, migration, adhesion, and force generation across diverse biological contexts. NM2 ...Nonmuscle myosin-2 (NM2) is a fundamental actin-based mechanochemical ATPase that regulates cellular architecture, migration, adhesion, and force generation across diverse biological contexts. NM2 function is tightly regulated by a structural transition between an autoinhibited monomeric (10S) conformation in which ATPase activity, actin binding, and filament assembly are coordinately suppressed and an enzymatically active, filamentous conformation. The autoinhibited conformation is critical for the spatial and temporal control of contractility in nonmuscle cells, yet structural insights into the 10S conformation remain largely elusive. Here, we report a ~53-nm elongated full-length structure of NM2B in the 10S conformation and four distinct cryo-EM structures representing the conformational landscape within the human NM2B 10S state. These structures reveal a tri-segmented tail fold that sequesters interfaces essential for actin binding and filament assembly. The asymmetric arrangement of myosin heavy and light chains provides a mechanistic foundation for understanding how regulatory post-translational modifications and disease-associated mutations shift NM2 conformational equilibria and may enable the development of structure-based interventions for cytoskeletal diseases including hearing loss, neurodegeneration, and cancer.
History
DepositionNov 8, 2025-
Header (metadata) releaseJul 8, 2026-
Map releaseJul 8, 2026-
UpdateJul 8, 2026-
Current statusJul 8, 2026Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_73797.png

Downloads & links

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Map

FileReleased
AnnotationComposite full-length 10S map
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.9 Å/pix.
x 512 pix.
= 975.201 Å		1.9 Å/pix.
x 512 pix.
= 975.201 Å		1.9 Å/pix.
x 512 pix.
= 975.201 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.90469 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.074
Minimum - Maximum-0.04287279 - 0.85744077
Average (Standard dev.)0.0011467726 (±0.012376862)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions512512512
Spacing512512512
CellA=B=C: 975.2013 Å
α=β=γ: 90.0 °

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Supplemental data

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Additional map: Head part of the full-length 10S map

Fileemd_73797_additional_1.map
AnnotationHead part of the full-length 10S map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Additional map: Tail part of the full-length 10S map

Fileemd_73797_additional_2.map
AnnotationTail part of the full-length 10S map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Nonmuscle myosin 2B

EntireName: Nonmuscle myosin 2B
Components
  • Complex: Nonmuscle myosin 2B
    • Protein or peptide: Myosin-10
    • Protein or peptide: Myosin light polypeptide 6
    • Protein or peptide: Myosin regulatory light chain 12B
  • Ligand: MAGNESIUM ION
  • Ligand: ADENOSINE-5'-DIPHOSPHATE
  • Ligand: PHOSPHATE ION

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Supramolecule #1: Nonmuscle myosin 2B

SupramoleculeName: Nonmuscle myosin 2B / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#3
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Myosin-10

MacromoleculeName: Myosin-10 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 229.361547 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MAQRTGLEDP ERYLFVDRAV IYNPATQADW TAKKLVWIPS ERHGFEAASI KEERGDEVMV ELAENGKKAM VNKDDIQKMN PPKFSKVED MAELTCLNEA SVLHNLKDRY YSGLIYTYSG LFCVVINPYK NLPIYSENII EMYRGKKRHE MPPHIYAISE S AYRCMLQD ...String:
MAQRTGLEDP ERYLFVDRAV IYNPATQADW TAKKLVWIPS ERHGFEAASI KEERGDEVMV ELAENGKKAM VNKDDIQKMN PPKFSKVED MAELTCLNEA SVLHNLKDRY YSGLIYTYSG LFCVVINPYK NLPIYSENII EMYRGKKRHE MPPHIYAISE S AYRCMLQD REDQSILCTG ESGAGKTENT KKVIQYLAHV ASSHKGRKDH NIPGELERQL LQANPILESF GNAKTVKNDN SS RFGKFIR INFDVTGYIV GANIETYLLE KSRAVRQAKD ERTFHIFYQL LSGAGEHLKS DLLLEGFNNY RFLSNGYIPI PGQ QDKDNF QETMEAMHIM GFSHEEILSM LKVVSSVLQF GNISFKKERN TDQASMPENT VAQKLCHLLG MNVMEFTRAI LTPR IKVGR DYVQKAQTKE QADFAVEALA KATYERLFRW LVHRINKALD RTKRQGASFI GILDIAGFEI FELNSFEQLC INYTN EKLQ QLFNHTMFIL EQEEYQREGI EWNFIDFGLD LQPCIDLIER PANPPGVLAL LDEECWFPKA TDKTFVEKLV QEQGSH SKF QKPRQLKDKA DFCIIHYAGK VDYKADEWLM KNMDPLNDNV ATLLHQSSDR FVAELWKDVD RIVGLDQVTG MTETAFG SA YKTKKGMFRT VGQLYKESLT KLMATLRNTN PNFVRCIIPN HEKRAGKLDP HLVLDQLRCN GVLEGIRICR QGFPNRIV F QEFRQRYEIL TPNAIPKGFM DGKQACERMI RALELDPNLY RIGQSKIFFR AGVLAHLEEE RDLKITDIII FFQAVCRGY LARKAFAKKQ QQLSALKVLQ RNCAAYLKLR HWQWWRVFTK VKPLLQVTRQ EEELQAKDEE LLKVKEKQTK VEGELEEMER KHQQLLEEK NILAEQLQAE TELFAEAEEM RARLAAKKQE LEEILHDLES RVEEEEERNQ ILQNEKKKMQ AHIQDLEEQL D EEEGARQK LQLEKVTAEA KIKKMEEEIL LLEDQNSKFI KEKKLMEDRI AECSSQLAEE EEKAKNLAKI RNKQEVMISD LE ERLKKEE KTRQELEKAK RKLDGETTDL QDQIAELQAQ IDELKLQLAK KEEELQGALA RGDDETLHKN NALKVVRELQ AQI AELQED FESEKASRNK AEKQKRDLSE ELEALKTELE DTLDTTAAQQ ELRTKREQEV AELKKALEEE TKNHEAQIQD MRQR HATAL EELSEQLEQA KRFKANLEKN KQGLETDNKE LACEVKVLQQ VKAESEHKRK KLDAQVQELH AKVSEGDRLR VELAE KASK LQNELDNVST LLEEAEKKGI KFAKDAASLE SQLQDTQELL QEETRQKLNL SSRIRQLEEE KNSLQEQQEE EEEARK NLE KQVLALQSQL ADTKKKVDDD LGTIESLEEA KKKLLKDAEA LSQRLEEKAL AYDKLEKTKN RLQQELDDLT VDLDHQR QV ASNLEKKQKK FDQLLAEEKS ISARYAEERD RAEAEAREKE TKALSLARAL EEALEAKEEF ERQNKQLRAD MEDLMSSK D DVGKNVHELE KSKRALEQQV EEMRTQLEEL EDELQATEDA KLRLEVNMQA MKAQFERDLQ TRDEQNEEKK RLLIKQVRE LEAELEDERK QRALAVASKK KMEIDLKDLE AQIEAANKAR DEVIKQLRKL QAQMKDYQRE LEEARASRDE IFAQSKESEK KLKSLEAEI LQLQEELASS ERARRHAEQE RDELADEITN SASGKSALLD EKRRLEARIA QLEEELEEEQ SNMELLNDRF R KTTLQVDT LNAELAAERS AAQKSDNARQ QLERQNKELK AKLQELEGAV KSKFKATISA LEAKIGQLEE QLEQEAKERA AA NKLVRRT EKKLKEIFMQ VEDERRHADQ YKEQMEKANA RMKQLKRQLE EAEEEATRAN ASRRKLQREL DDATEANEGL SRE VSTLKN RLRRGGPISF SSSRSGRRQL HLEGASLELS DDDTESKTSD VNETQPPQSE

UniProtKB: Myosin-10

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Macromolecule #2: Myosin light polypeptide 6

MacromoleculeName: Myosin light polypeptide 6 / type: protein_or_peptide / ID: 2 / Details: ELC / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 16.948031 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString:
MCDFTEDQTA EFKEAFQLFD RTGDGKILYS QCGDVMRALG QNPTNAEVLK VLGNPKSDEM NVKVLDFEHF LPMLQTVAKN KDQGTYEDY VEGLRVFDKE GNGTVMGAEI RHVLVTLGEK MTEEEVEMLV AGHEDSNGCI NYEAFVRHIL SG

UniProtKB: Myosin light polypeptide 6

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Macromolecule #3: Myosin regulatory light chain 12B

MacromoleculeName: Myosin regulatory light chain 12B / type: protein_or_peptide / ID: 3 / Details: RLC / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 19.80416 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString:
MSSKKAKTKT TKKRPQRATS NVFAMFDQSQ IQEFKEAFNM IDQNRDGFID KEDLHDMLAS LGKNPTDAYL DAMMNEAPGP INFTMFLTM FGEKLNGTDP EDVIRNAFAC FDEEATGTIQ EDYLRELLTT MGDRFTDEEV DELYREAPID KKGNFNYIEF T RILKHGAK DKDD

UniProtKB: Myosin regulatory light chain 12B

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Macromolecule #4: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 4 / Number of copies: 2 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Macromolecule #5: ADENOSINE-5'-DIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 5 / Number of copies: 2 / Formula: ADP
Molecular weightTheoretical: 427.201 Da
Chemical component information

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

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Macromolecule #6: PHOSPHATE ION

MacromoleculeName: PHOSPHATE ION / type: ligand / ID: 6 / Number of copies: 2 / Formula: PO4
Molecular weightTheoretical: 94.971 Da
Chemical component information

ChemComp-PO4:
PHOSPHATE ION

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.4
GridModel: C-flat-1.2/1.3 / Material: GOLD / Mesh: 300 / Pretreatment - Type: GLOW DISCHARGE
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Specialist opticsEnergy filter - Slit width: 20 eV
Image recordingFilm or detector model: GATAN K2 QUANTUM (4k x 4k) / Average electron dose: 72.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.5 µm / Nominal defocus min: 1.5 µm / Nominal magnification: 130000
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: OTHER / Details: 7MF3 and AlphaFold
Final reconstructionResolution.type: BY AUTHOR / Resolution: 10.0 Å / Resolution method: OTHER / Software - Name: cryoSPARC
Details: It is a composite map of the head and tail domains.
Number images used: 38939
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC

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Atomic model buiding 1

Initial modelChain - Source name: Other / Chain - Initial model type: other / Details: 7MF3 and AlphaFold
RefinementProtocol: RIGID BODY FIT
Output model

PDB-9z40:
Cryo-EM structure of full-length human NM2B

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