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- EMDB-43923: Bovine fetal muscle nAChR bound to ACh -

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Basic information

Entry
Database: EMDB / ID: EMD-43923
TitleBovine fetal muscle nAChR bound to ACh
Map datasharp
Sample
  • Complex: Bovine muscle nicotinic acetylcholine receptor
    • Protein or peptide: Acetylcholine receptor subunit alpha
    • Protein or peptide: Acetylcholine receptor subunit beta
    • Protein or peptide: Acetylcholine receptor subunit delta
    • Protein or peptide: Acetylcholine receptor subunit gamma
  • Ligand: (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate
  • Ligand: ACETYLCHOLINE
  • Ligand: water
KeywordsBovine muscle nicotinic acetylcholine receptor / MEMBRANE PROTEIN
Function / homology
Function and homology information


Highly sodium permeable postsynaptic acetylcholine nicotinic receptors / Highly calcium permeable postsynaptic nicotinic acetylcholine receptors / Highly calcium permeable nicotinic acetylcholine receptors / postsynaptic membrane organization / skeletal muscle tissue growth / musculoskeletal movement / acetylcholine receptor activity / excitatory extracellular ligand-gated monoatomic ion channel activity / acetylcholine-gated channel complex / behavioral response to nicotine ...Highly sodium permeable postsynaptic acetylcholine nicotinic receptors / Highly calcium permeable postsynaptic nicotinic acetylcholine receptors / Highly calcium permeable nicotinic acetylcholine receptors / postsynaptic membrane organization / skeletal muscle tissue growth / musculoskeletal movement / acetylcholine receptor activity / excitatory extracellular ligand-gated monoatomic ion channel activity / acetylcholine-gated channel complex / behavioral response to nicotine / neuromuscular synaptic transmission / acetylcholine-gated monoatomic cation-selective channel activity / muscle cell development / acetylcholine binding / synaptic transmission, cholinergic / nervous system process / acetylcholine receptor signaling pathway / postsynaptic specialization membrane / monoatomic cation transport / membrane depolarization / muscle contraction / response to nicotine / transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential / neuromuscular junction / transmembrane signaling receptor activity / channel activity / monoatomic ion transmembrane transport / chemical synaptic transmission / postsynaptic membrane / neuron projection / synapse / signal transduction / plasma membrane
Similarity search - Function
Nicotinic acetylcholine receptor / Neurotransmitter-gated ion-channel, conserved site / Neurotransmitter-gated ion-channels signature. / Neurotransmitter-gated ion-channel transmembrane domain / Neurotransmitter-gated ion-channel transmembrane region / Neurotransmitter-gated ion-channel transmembrane domain superfamily / Neuronal acetylcholine receptor / Neurotransmitter-gated ion-channel / Neurotransmitter-gated ion-channel ligand-binding domain / Neurotransmitter-gated ion-channel ligand-binding domain superfamily / Neurotransmitter-gated ion-channel ligand binding domain
Similarity search - Domain/homology
Acetylcholine receptor subunit alpha / Acetylcholine receptor subunit beta / Acetylcholine receptor subunit delta / Acetylcholine receptor subunit gamma
Similarity search - Component
Biological speciesBos taurus (domestic cattle)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.45 Å
AuthorsLi H / Hibbs RE
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of Neurological Disorders and Stroke (NIH/NINDS) United States
CitationJournal: Nature / Year: 2024
Title: Structural switch in acetylcholine receptors in developing muscle.
Authors: Huanhuan Li / Jinfeng Teng / Ryan E Hibbs /
Abstract: During development, motor neurons originating in the brainstem and spinal cord form elaborate synapses with skeletal muscle fibres. These neurons release acetylcholine (ACh), which binds to nicotinic ...During development, motor neurons originating in the brainstem and spinal cord form elaborate synapses with skeletal muscle fibres. These neurons release acetylcholine (ACh), which binds to nicotinic ACh receptors (AChRs) on the muscle, initiating contraction. Two types of AChR are present in developing muscle cells, and their differential expression serves as a hallmark of neuromuscular synapse maturation. The structural principles underlying the switch from fetal to adult muscle receptors are unknown. Here, we present high-resolution structures of both fetal and adult muscle nicotinic AChRs, isolated from bovine skeletal muscle in developmental transition. These structures, obtained in the absence and presence of ACh, provide a structural context for understanding how fetal versus adult receptor isoforms are tuned for synapse development versus the all-or-none signalling required for high-fidelity skeletal muscle contraction. We find that ACh affinity differences are driven by binding site access, channel conductance is tuned by widespread surface electrostatics and open duration changes result from intrasubunit interactions and structural flexibility. The structures further reveal pathogenic mechanisms underlying congenital myasthenic syndromes.
History
DepositionMar 5, 2024-
Header (metadata) releaseJul 31, 2024-
Map releaseJul 31, 2024-
UpdateMay 21, 2025-
Current statusMay 21, 2025Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_43923.png

Downloads & links

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Map

FileDownload / File: emd_43923.map.gz / Format: CCP4 / Size: 512 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotationsharp
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.94 Å/pix.
x 512 pix.
= 478.72 Å		0.94 Å/pix.
x 512 pix.
= 478.72 Å		0.94 Å/pix.
x 512 pix.
= 478.72 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.935 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.03
Minimum - Maximum-0.30559704 - 0.5806587
Average (Standard dev.)-0.000029759522 (±0.0066215405)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions512512512
Spacing512512512
CellA=B=C: 478.72 Å
α=β=γ: 90.0 °

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Supplemental data

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Additional map: emhancer

Fileemd_43923_additional_1.map
Annotationemhancer
Projections & Slices
AxesZYX

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Slices (1/2)
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Additional map: unsharp

Fileemd_43923_additional_2.map
Annotationunsharp
Projections & Slices
AxesZYX

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Slices (1/2)
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Histogram

Histogram (log scale)

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Half map: fetal desen halfmapA

Fileemd_43923_half_map_1.map
Annotationfetal_desen_halfmapA
Projections & Slices
AxesZYX

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Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: fetal desen halfmapB

Fileemd_43923_half_map_2.map
Annotationfetal_desen_halfmapB
Projections & Slices
AxesZYX

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Sample components

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Entire : Bovine muscle nicotinic acetylcholine receptor

EntireName: Bovine muscle nicotinic acetylcholine receptor
Components
  • Complex: Bovine muscle nicotinic acetylcholine receptor
    • Protein or peptide: Acetylcholine receptor subunit alpha
    • Protein or peptide: Acetylcholine receptor subunit beta
    • Protein or peptide: Acetylcholine receptor subunit delta
    • Protein or peptide: Acetylcholine receptor subunit gamma
  • Ligand: (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate
  • Ligand: ACETYLCHOLINE
  • Ligand: water

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Supramolecule #1: Bovine muscle nicotinic acetylcholine receptor

SupramoleculeName: Bovine muscle nicotinic acetylcholine receptor / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#4
Source (natural)Organism: Bos taurus (domestic cattle)

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Macromolecule #1: Acetylcholine receptor subunit alpha

MacromoleculeName: Acetylcholine receptor subunit alpha / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (domestic cattle)
Molecular weightTheoretical: 49.949828 KDa
SequenceString: SEHETRLVAK LFEDYNSVVR PVEDHRQAVE VTVGLQLIQL INVDEVNQIV TTNVRLKQQW VDYNLKWNPD DYGGVKKIHI PSEKIWRPD LVLYNNADGD FAIVKFTKVL LDYTGHITWT PPAIFKSYCE IIVTHFPFDE QNCSMKLGTW TYDGSVVVIN P ESDQPDLS ...String:
SEHETRLVAK LFEDYNSVVR PVEDHRQAVE VTVGLQLIQL INVDEVNQIV TTNVRLKQQW VDYNLKWNPD DYGGVKKIHI PSEKIWRPD LVLYNNADGD FAIVKFTKVL LDYTGHITWT PPAIFKSYCE IIVTHFPFDE QNCSMKLGTW TYDGSVVVIN P ESDQPDLS NFMESGEWVI KESRGWKHWV FYACCPSTPY LDITYHFVMQ RLPLYFIVNV IIPCLLFSFL TGLVFYLPTD SG EKMTLSI SVLLSLTVFL LVIVELIPST SSAVPLIGKY MLFTMVFVIA SIIITVIVIN THHRSPSTHV MPEWVRKVFI DTI PNIMFF STMKRPSREK QDKKIFTEDI DISDISGKPG PPPMGFHSPL IKHPEVKSAI EGIKYIAETM KSDQESNNAA EEWK YVAMV MDHILLAVFM LVCIIGTLAV FAGRLIELNQ QG

UniProtKB: Acetylcholine receptor subunit alpha

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Macromolecule #2: Acetylcholine receptor subunit beta

MacromoleculeName: Acetylcholine receptor subunit beta / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (domestic cattle)
Molecular weightTheoretical: 55.111832 KDa
SequenceString: SEAEGRLREK LFSGYDSTVR PAREVGDRVW VSIGLTLAQL ISLNEKDEEM STKVYLDLEW TDYRLSWDPE EHEGIDSLRI SAESVWLPD VVLLNNNDGN FDVALDINVV VSSDGSMRWQ PPGIYRSSCS IQVTYFPFDW QNCTMVFSSY SYDSSEVSLQ T GLSPEGQE ...String:
SEAEGRLREK LFSGYDSTVR PAREVGDRVW VSIGLTLAQL ISLNEKDEEM STKVYLDLEW TDYRLSWDPE EHEGIDSLRI SAESVWLPD VVLLNNNDGN FDVALDINVV VSSDGSMRWQ PPGIYRSSCS IQVTYFPFDW QNCTMVFSSY SYDSSEVSLQ T GLSPEGQE RQEVYIHEGT FIENGQWEII HKPSRLIQPS VDPRGGGEGR REEVTFYLII RRKPLFYLVN VIAPCILITL LA IFVFYLP PDAGEKMGLS IFALLTLTVF LLLLADKVPE TSLSVPIIIK YLMFTMVLVT FSVILSVVVL NLHHRSPHTH QMP LWVRQI FIHKLPLYLG LKRPKPERDQ MQEPPSIAPR DSPGSGWGRG TDEYFIRKPP NDFLFPKPNR FQPELSAPDL RRFI DGPNR AVGLPPELRE VVSSISYIAR QLQEQEDHDV LKEDWQFVAM VVDRLFLWTF IIFTSVGTLV IFLDATYHLP PADPF P

UniProtKB: Acetylcholine receptor subunit beta

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Macromolecule #3: Acetylcholine receptor subunit delta

MacromoleculeName: Acetylcholine receptor subunit delta / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (domestic cattle)
Molecular weightTheoretical: 56.543926 KDa
SequenceString: LNEEERLIRH LFEEKAYNKE LRPAAHKESV EISLALTLSN LISLKEVEET LTTNVWIEQG WTDSRLQWDA EDFGNISVLR LPADMVWLP EIVLENNNDG SFQISYSCNV LIYPSGSVYW LPPAIFRSSC PISVTYFPFD WQNCSLKFSS LKYTTKEITL S LKQAEEDG ...String:
LNEEERLIRH LFEEKAYNKE LRPAAHKESV EISLALTLSN LISLKEVEET LTTNVWIEQG WTDSRLQWDA EDFGNISVLR LPADMVWLP EIVLENNNDG SFQISYSCNV LIYPSGSVYW LPPAIFRSSC PISVTYFPFD WQNCSLKFSS LKYTTKEITL S LKQAEEDG RSYPVEWIII DPEGFTENGE WEIVHRPARV NVDPSVPLDS PNRQDVTFYL IIRRKPLFYV INILVPCVLI SF MINLVFY LPADCGEKTS MAISVLLAQS VFLLLISKRL PATSMAIPLI GKFLLFGMVL VTMVVVICVI VLNIHFRTPS THV LSEPVK KLFLETLPEI LHMSRPAEDG PSPGTLIRRS SSLGYISKAE EYFSLKSRSD LMFEKQSERH GLARRLTTAR RPPA GSEQA QQELFSELKP AVDGANFIVN HMKDQNNYNE EKDCWNRVAR TVDRLCLFVV TPIMVVGTAW IFLQGAYNQP PPQPF PGDP FSYLEKDKRF I

UniProtKB: Acetylcholine receptor subunit delta

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Macromolecule #4: Acetylcholine receptor subunit gamma

MacromoleculeName: Acetylcholine receptor subunit gamma / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Bos taurus (domestic cattle)
Molecular weightTheoretical: 55.99468 KDa
SequenceString: RNQEERLLGD LMQGYNPHLR PAEHDSDVVN VSLKLTLTNL ISLNEREEAL TTNVWIEMQW CDYRLRWDPR DYGGLWVLRV PSTMVWRPD IVLENNVDGV FEVALYCNVL VSPDGCVYWL PPAIFRSSCP VSVTFFPFDW QNCSLIFQSQ TYSTNEINLQ L SQEDGQTI ...String:
RNQEERLLGD LMQGYNPHLR PAEHDSDVVN VSLKLTLTNL ISLNEREEAL TTNVWIEMQW CDYRLRWDPR DYGGLWVLRV PSTMVWRPD IVLENNVDGV FEVALYCNVL VSPDGCVYWL PPAIFRSSCP VSVTFFPFDW QNCSLIFQSQ TYSTNEINLQ L SQEDGQTI EWIFIDPEAF TENGEWAIRH RPAKMLLDEA APAEEAGHQK VVFYLLIQRK PLFYVINIIA PCVLISSVAI LI YFLPAKA GGQKCTVAIN VLLAQTVFLF LVAKKVPETS QAVPLISKYL TFLLVVTILI VVNAVVVLNV SLRSPHTHSM ARG VRKVFL RLLPQLLRMH VRPLAPVAVQ DAHPRLQNGS SSGWPITAGE EVALCLPRSE LLFRQRQRNG LVRAALEKLE KGPE SGQSP EWCGSLKQAA PAIQACVEAC NLIARARHQQ THFDSGNKEW FLVGRVLDRV CFLAMLSLFV CGTAGIFLMA HYNRV PALP FPGDPRSYLP SSD

UniProtKB: Acetylcholine receptor subunit gamma

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Macromolecule #10: (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(tri...

MacromoleculeName: (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate
type: ligand / ID: 10 / Number of copies: 2 / Formula: POV
Molecular weightTheoretical: 760.076 Da
Chemical component information

ChemComp-POV:
(2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate / phospholipid*YM

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Macromolecule #11: ACETYLCHOLINE

MacromoleculeName: ACETYLCHOLINE / type: ligand / ID: 11 / Number of copies: 2 / Formula: ACH
Molecular weightTheoretical: 146.207 Da
Chemical component information

ChemComp-ACH:
ACETYLCHOLINE

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Macromolecule #12: water

MacromoleculeName: water / type: ligand / ID: 12 / Number of copies: 5 / Formula: HOH
Molecular weightTheoretical: 18.015 Da
Chemical component information

ChemComp-HOH:
WATER

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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
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: FEI FALCON III (4k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: OTHER / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.6 µm
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
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.45 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 259740
Initial angle assignmentType: ANGULAR RECONSTITUTION
Final angle assignmentType: ANGULAR RECONSTITUTION
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial modelChain - Source name: Other / Chain - Initial model type: experimental model / Details: cryosparc ab initial model
RefinementSpace: REAL / Protocol: AB INITIO MODEL
Output model

PDB-9avu:
Bovine fetal muscle nAChR bound to ACh

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