7PO4
Assembly intermediate of human mitochondrial ribosome large subunit (largely unfolded rRNA with MALSU1, L0R8F8 and ACP)
This is a non-PDB format compatible entry.
Summary for 7PO4
| Entry DOI | 10.2210/pdb7po4/pdb |
| EMDB information | 13562 |
| Descriptor | 16SrRNA, 39S ribosomal protein L14, mitochondrial, 39S ribosomal protein L15, mitochondrial, ... (61 entities in total) |
| Functional Keywords | small subunit, mitochondrion, biogenesis, maturation, ribosome |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 60 |
| Total formula weight | 1911856.54 |
| Authors | Itoh, Y.,Khawaja, A.,Rorbach, J.,Amunts, A. (deposition date: 2021-09-08, release date: 2022-06-15, Last modification date: 2023-11-15) |
| Primary citation | Itoh, Y.,Khawaja, A.,Laptev, I.,Cipullo, M.,Atanassov, I.,Sergiev, P.,Rorbach, J.,Amunts, A. Mechanism of mitoribosomal small subunit biogenesis and preinitiation. Nature, 606:603-608, 2022 Cited by PubMed Abstract: Mitoribosomes are essential for the synthesis and maintenance of bioenergetic proteins. Here we use cryo-electron microscopy to determine a series of the small mitoribosomal subunit (SSU) intermediates in complex with auxiliary factors, revealing a sequential assembly mechanism. The methyltransferase TFB1M binds to partially unfolded rRNA h45 that is promoted by RBFA, while the mRNA channel is blocked. This enables binding of METTL15 that promotes further rRNA maturation and a large conformational change of RBFA. The new conformation allows initiation factor mtIF3 to already occupy the subunit interface during the assembly. Finally, the mitochondria-specific ribosomal protein mS37 (ref. ) outcompetes RBFA to complete the assembly with the SSU-mS37-mtIF3 complex that proceeds towards mtIF2 binding and translation initiation. Our results explain how the action of step-specific factors modulate the dynamic assembly of the SSU, and adaptation of a unique protein, mS37, links the assembly to initiation to establish the catalytic human mitoribosome. PubMed: 35676484DOI: 10.1038/s41586-022-04795-x PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.56 Å) |
Structure validation
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