8t06 | pdb_00008t06

Structure of mouse Myomaker mutant-R107A bound to Fab18G7

spinqualitylabelsall models 8t06, resolution 3.32Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8t06 is a 6 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.32Å Ligands: ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MYMK_MOUSE Myoblast-specific protein that mediates myoblast fusion, an essential step for the formation of multi-nucleated muscle fibers (PubMed:23868259, PubMed:28386024, PubMed:28681861, PubMed:30197239). Actively participates in the membrane fusion reaction by mediating the mixing of cell membrane lipids (hemifusion) upstream of MYMX (PubMed:30197239). Acts independently of MYMX (PubMed:30197239). Involved in skeletal muscle regeneration in response to injury by mediating the fusion of satellite cells, a population of muscle stem cells, with injured myofibers (PubMed:25085416). Also involved in skeletal muscle hypertrophy, probably by mediating the fusion of satellite cells with myofibers (PubMed:28186492). Publication Abstract from PubMed 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. Cryo-EM structures of Myomaker reveal a molecular basis for myoblast fusion.,Long T, Zhang Y, Donnelly L, Li H, Pien YC, Liu N, Olson EN, Li X Nat Struct Mol Biol. 2023 Nov;30(11):1746-1754. doi: 10.1038/s41594-023-01110-8. , Epub 2023 Sep 28. PMID:37770716 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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