+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-40933 | |||||||||
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Title | Structure of mouse Myomaker bound to Fab18G7 in detergent | |||||||||
Map data | ||||||||||
Sample |
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Keywords | MEMBRANE 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 | |||||||||
Biological species | Mus musculus (house mouse) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.72 Å | |||||||||
Authors | Long T / Li X | |||||||||
Funding support | United States, 1 items
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Citation | Journal: 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 |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_40933.map.gz | 97 MB | EMDB map data format | |
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Header (meta data) | emd-40933-v30.xml emd-40933.xml | 17.7 KB 17.7 KB | Display Display | EMDB header |
Images | emd_40933.png | 47.3 KB | ||
Masks | emd_40933_msk_1.map | 103 MB | Mask map | |
Filedesc metadata | emd-40933.cif.gz | 5.9 KB | ||
Others | emd_40933_half_map_1.map.gz emd_40933_half_map_2.map.gz | 95.5 MB 95.5 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-40933 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-40933 | HTTPS FTP |
-Validation report
Summary document | emd_40933_validation.pdf.gz | 885.5 KB | Display | EMDB validaton report |
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Full document | emd_40933_full_validation.pdf.gz | 885.1 KB | Display | |
Data in XML | emd_40933_validation.xml.gz | 13.3 KB | Display | |
Data in CIF | emd_40933_validation.cif.gz | 15.5 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-40933 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-40933 | HTTPS FTP |
-Related structure data
Related structure data | 8t03MC 8t04C 8t05C 8t06C 8t07C M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_40933.map.gz / Format: CCP4 / Size: 103 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
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
File | emd_40933_msk_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_40933_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_40933_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
+Entire : Complex of mouse Myomaker and Fab18G7
+Supramolecule #1: Complex of mouse Myomaker and Fab18G7
+Supramolecule #2: Mouse Myomaker
+Supramolecule #3: Fab18G7
+Macromolecule #1: Protein myomaker
+Macromolecule #2: 18G7 Fab heavy chain
+Macromolecule #3: 18G7 Fab light chain
+Macromolecule #4: ZINC ION
+Macromolecule #5: CHOLESTEROL
+Macromolecule #6: 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine
+Macromolecule #7: water
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.5 |
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Vitrification | Cryogen name: ETHANE |
-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: FIELD EMISSION GUN |
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 |
-Image processing
Startup model | Type of model: OTHER |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 2.72 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 371611 |
Initial angle assignment | Type: NOT APPLICABLE |
Final angle assignment | Type: NOT APPLICABLE |