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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | Structure of mouse Myomaker mutant-Y118A bound to Fab18G7 | |||||||||
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![]() | MEMBRANE PROTEIN | |||||||||
Function / homology | ![]() 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 | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.38 Å | |||||||||
![]() | Long T / Li X | |||||||||
Funding support | ![]()
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![]() | ![]() 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 |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 97.1 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 16.7 KB 16.7 KB | Display Display | ![]() |
Images | ![]() | 49.4 KB | ||
Masks | ![]() | 103 MB | ![]() | |
Filedesc metadata | ![]() | 5.6 KB | ||
Others | ![]() ![]() | 95.3 MB 95.3 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 942.9 KB | Display | ![]() |
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Full document | ![]() | 942.5 KB | Display | |
Data in XML | ![]() | 13.3 KB | Display | |
Data in CIF | ![]() | 15.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8t07MC ![]() 8t03C ![]() 8t04C ![]() 8t05C ![]() 8t06C M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Map
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Voxel size | X=Y=Z: 0.83 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
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Density Histograms |
-Half map: #2
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_40937_half_map_2.map | ||||||||||||
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Density Histograms |
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Sample components
-Entire : Complex of mouse Myomaker mutant-Y118A with Fab18G7
Entire | Name: Complex of mouse Myomaker mutant-Y118A with Fab18G7 |
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Components |
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-Supramolecule #1: Complex of mouse Myomaker mutant-Y118A with Fab18G7
Supramolecule | Name: Complex of mouse Myomaker mutant-Y118A with Fab18G7 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#3 |
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-Supramolecule #2: mouse Myomaker mutant-Y118A
Supramolecule | Name: mouse Myomaker mutant-Y118A / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1 |
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Source (natural) | Organism: ![]() ![]() |
-Supramolecule #3: Fab18G7
Supramolecule | Name: Fab18G7 / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #2-#3 |
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Source (natural) | Organism: ![]() ![]() |
-Macromolecule #1: Protein myomaker
Macromolecule | Name: Protein myomaker / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 24.725371 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MGTVVAKLLL PTLSSLAFLP TVSIATKRRF YMEAMVYLFT MFFVAFSHAC DGPGLSVLCF MRRDILEYFS IYGTALSMWV SLMALADFD EPQRSTFTML GVLTIAVRTF HDRWGYGVAS GPIGTATLII AVKWLKKMKE KKGLYPDKSI YTQQIGPGLC F GALALMLR ...String: MGTVVAKLLL PTLSSLAFLP TVSIATKRRF YMEAMVYLFT MFFVAFSHAC DGPGLSVLCF MRRDILEYFS IYGTALSMWV SLMALADFD EPQRSTFTML GVLTIAVRTF HDRWGYGVAS GPIGTATLII AVKWLKKMKE KKGLYPDKSI YTQQIGPGLC F GALALMLR FFFEEWDYTY VHSFYHCALA MSFVLLLPKV NKKAGNAGAP AKLTFSTLCC TCV UniProtKB: Protein myomaker |
-Macromolecule #2: 18G7 Fab heavy chain
Macromolecule | Name: 18G7 Fab heavy chain / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 13.318994 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: QVTLKESGPG ILQPSQTLSL TCSFSGFSLS TSGMGVSWIR KPSGKGLEWL AHIFWDDDKR YNPSLKSRLT ISKDTSSNQV FLMITSIDT ADTATYYCAR RTWLLHAMDY WGQGTSVTVS S |
-Macromolecule #3: 18G7 Fab light chain
Macromolecule | Name: 18G7 Fab light chain / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 11.809201 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: DIQMTQSPSS LSASLGGKVT ITCKASQDIN EYIAWYQHKP GKGPRLLIHY TSTLQPGIPS RFSGSGSGRD YSFSISNLEP EDIATYYCL QYDNLLWTFG GGTKLEIK |
-Macromolecule #4: ZINC ION
Macromolecule | Name: ZINC ION / type: ligand / ID: 4 / Number of copies: 2 / Formula: ZN |
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Molecular weight | Theoretical: 65.409 Da |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.5 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 60.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.8 µm / Nominal defocus min: 0.8 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Startup model | Type of model: OTHER |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.38 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 124683 |
Initial angle assignment | Type: NOT APPLICABLE |
Final angle assignment | Type: NOT APPLICABLE |