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- PDB-8t03: Structure of mouse Myomaker bound to Fab18G7 in detergent -

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Basic information

Entry
Database: PDB / ID: 8t03
TitleStructure of mouse Myomaker bound to Fab18G7 in detergent
Components
  • 18G7 Fab heavy chain
  • 18G7 Fab light chain
  • Protein myomaker
KeywordsMEMBRANE PROTEIN
Function / homology
Function and homology information


positive regulation of skeletal muscle hypertrophy / plasma membrane fusion / myoblast fusion involved in skeletal muscle regeneration / skeletal muscle tissue regeneration / myoblast fusion / muscle organ development / Golgi membrane / plasma membrane
Similarity search - Function
NGX6/PGAP6/MYMK / Protein of unknown function (DUF3522)
Similarity search - Domain/homology
CHOLESTEROL / 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine / Protein myomaker
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.72 Å
AuthorsLong, T. / Li, X.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM135343 United States
CitationJournal: Nat Struct Mol Biol / Year: 2023
Title: Cryo-EM structures of Myomaker reveal a molecular basis for myoblast fusion.
Authors: Tao Long / Yichi Zhang / Linda Donnelly / Hui Li / Yu-Chung Pien / Ning Liu / Eric N Olson / Xiaochun Li /
Abstract: The fusion of mononucleated myoblasts produces multinucleated muscle fibers leading to the formation of skeletal muscle. Myomaker, a skeletal muscle-specific membrane protein, is essential for ...The fusion of mononucleated myoblasts produces multinucleated muscle fibers leading to the formation of skeletal muscle. Myomaker, a skeletal muscle-specific membrane protein, is essential for myoblast fusion. Here we report the cryo-EM structures of mouse Myomaker (mMymk) and Ciona robusta Myomaker (cMymk). Myomaker contains seven transmembrane helices (TMs) that adopt a G-protein-coupled receptor-like fold. TMs 2-4 form a dimeric interface, while TMs 3 and 5-7 create a lipid-binding site that holds the polar head of a phospholipid and allows the alkyl tails to insert into Myomaker. The similarity of cMymk and mMymk suggests a conserved Myomaker-mediated cell fusion mechanism across evolutionarily distant species. Functional analyses demonstrate the essentiality of the dimeric interface and the lipid-binding site for fusogenic activity, and heterologous cell-cell fusion assays show the importance of transcellular interactions of Myomaker protomers for myoblast fusion. Together, our findings provide structural and functional insights into the process of myoblast fusion.
History
DepositionMay 31, 2023Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 27, 2023Provider: repository / Type: Initial release
Revision 1.1Oct 4, 2023Group: Database references / Category: citation_author
Revision 1.2Oct 11, 2023Group: Database references / Category: citation / citation_author
Item: _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.name
Revision 1.3Nov 22, 2023Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation_author.identifier_ORCID

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Protein myomaker
B: Protein myomaker
C: 18G7 Fab heavy chain
D: 18G7 Fab light chain
E: 18G7 Fab heavy chain
F: 18G7 Fab light chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)102,31612
Polymers99,8916
Non-polymers2,4246
Water724
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

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Protein , 1 types, 2 molecules AB

#1: Protein Protein myomaker / Myoblast fusion maker / Transmembrane protein 8C


Mass: 24817.469 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Mymk, Tmem8c / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: Q9D1N4

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Antibody , 2 types, 4 molecules CEDF

#2: Antibody 18G7 Fab heavy chain


Mass: 13318.994 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Production host: Homo sapiens (human)
#3: Antibody 18G7 Fab light chain


Mass: 11809.201 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Production host: Homo sapiens (human)

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Non-polymers , 4 types, 10 molecules

#4: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Formula: Zn
#5: Chemical ChemComp-CLR / CHOLESTEROL / Cholesterol


Mass: 386.654 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C27H46O
#6: Chemical ChemComp-LBN / 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine / (2R)-2-[(9Z)-9-Octadecenoyloxy]-3-(palmitoyloxy)propyl 2-(trimethylammonio)ethyl phosphate / POPC


Mass: 760.076 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C42H82NO8P / Feature type: SUBJECT OF INVESTIGATION / Comment: phospholipid*YM
#7: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestY

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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

Component
IDNameTypeEntity IDParent-IDSource
1Complex of mouse Myomaker and Fab18G7COMPLEX#1-#30MULTIPLE SOURCES
2Mouse MyomakerCOMPLEX#11RECOMBINANT
3Fab18G7COMPLEX#2-#31RECOMBINANT
Source (natural)
IDEntity assembly-IDOrganismNcbi tax-ID
22Mus musculus (house mouse)10090
33Mus musculus (house mouse)10090
Source (recombinant)
IDEntity assembly-IDOrganismNcbi tax-ID
22Spodoptera frugiperda (fall armyworm)7108
33Homo sapiens (human)9606
Buffer solutionpH: 7.5
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 1800 nm / Nominal defocus min: 800 nm
Image recordingElectron dose: 60 e/Å2 / Film or detector model: GATAN K3 (6k x 4k)

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Processing

EM softwareName: REFMAC / Version: 5.8.0267 / Category: model refinement
CTF correctionType: NONE
3D reconstructionResolution: 2.72 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 371611 / Symmetry type: POINT
RefinementResolution: 2.72→249 Å / Cor.coef. Fo:Fc: 0.787 / Cor.coef. Fo:Fc free: 0.788 / SU B: 6.548 / SU ML: 0.111 / Cross valid method: THROUGHOUT / ESU R: 0.074 / ESU R Free: 0.074 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.39886 81182 5.1 %RANDOM
Rwork0.3967 ---
obs0.39681 1525727 100 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 99.495 Å2
Baniso -1Baniso -2Baniso -3
1-1.51 Å21.94 Å20.01 Å2
2--1.23 Å20 Å2
3----2.74 Å2
Refinement stepCycle: 1 / Total: 6878
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
ELECTRON MICROSCOPYr_bond_refined_d0.0030.0137062
ELECTRON MICROSCOPYr_bond_other_d0.0010.0156706
ELECTRON MICROSCOPYr_angle_refined_deg1.3491.6429572
ELECTRON MICROSCOPYr_angle_other_deg1.0841.5715486
ELECTRON MICROSCOPYr_dihedral_angle_1_deg8.8425846
ELECTRON MICROSCOPYr_dihedral_angle_2_deg31.92421.133300
ELECTRON MICROSCOPYr_dihedral_angle_3_deg14.087151158
ELECTRON MICROSCOPYr_dihedral_angle_4_deg15.6471532
ELECTRON MICROSCOPYr_chiral_restr0.0590.2922
ELECTRON MICROSCOPYr_gen_planes_refined0.0040.027684
ELECTRON MICROSCOPYr_gen_planes_other0.0020.021638
ELECTRON MICROSCOPYr_nbd_refined
ELECTRON MICROSCOPYr_nbd_other
ELECTRON MICROSCOPYr_nbtor_refined
ELECTRON MICROSCOPYr_nbtor_other
ELECTRON MICROSCOPYr_xyhbond_nbd_refined
ELECTRON MICROSCOPYr_xyhbond_nbd_other
ELECTRON MICROSCOPYr_metal_ion_refined
ELECTRON MICROSCOPYr_metal_ion_other
ELECTRON MICROSCOPYr_symmetry_vdw_refined
ELECTRON MICROSCOPYr_symmetry_vdw_other
ELECTRON MICROSCOPYr_symmetry_hbond_refined
ELECTRON MICROSCOPYr_symmetry_hbond_other
ELECTRON MICROSCOPYr_symmetry_metal_ion_refined
ELECTRON MICROSCOPYr_symmetry_metal_ion_other
ELECTRON MICROSCOPYr_mcbond_it1.00610.8153402
ELECTRON MICROSCOPYr_mcbond_other1.00610.8143401
ELECTRON MICROSCOPYr_mcangle_it1.89916.2154242
ELECTRON MICROSCOPYr_mcangle_other1.89916.2164243
ELECTRON MICROSCOPYr_scbond_it0.49110.6383660
ELECTRON MICROSCOPYr_scbond_other0.49110.6383660
ELECTRON MICROSCOPYr_scangle_it
ELECTRON MICROSCOPYr_scangle_other1.0215.9585330
ELECTRON MICROSCOPYr_long_range_B_refined3.3517533
ELECTRON MICROSCOPYr_long_range_B_other3.357534
ELECTRON MICROSCOPYr_rigid_bond_restr
ELECTRON MICROSCOPYr_sphericity_free
ELECTRON MICROSCOPYr_sphericity_bonded
LS refinement shellResolution: 2.72→2.791 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree2.504 5871 -
Rwork2.478 113497 -
obs--100 %

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