7O9M
Human mitochondrial ribosome large subunit assembly intermediate with MTERF4-NSUN4, MRM2, MTG1 and the MALSU module
This is a non-PDB format compatible entry.
Summary for 7O9M
| Entry DOI | 10.2210/pdb7o9m/pdb |
| EMDB information | 12764 |
| Descriptor | 16S rRNA, 39S ribosomal protein L13, mitochondrial, 39S ribosomal protein L14, mitochondrial, ... (66 entities in total) |
| Functional Keywords | mitochondria, gtpase, ribosome assembly intermediate, ribosome |
| Biological source | Homo sapiens More |
| Total number of polymer chains | 66 |
| Total formula weight | 2078393.58 |
| Authors | |
| Primary citation | Cipullo, M.,Gese, G.V.,Khawaja, A.,Hallberg, B.M.,Rorbach, J. Structural basis for late maturation steps of the human mitoribosomal large subunit. Nat Commun, 12:3673-3673, 2021 Cited by PubMed Abstract: Mitochondrial ribosomes (mitoribosomes) synthesize a critical set of proteins essential for oxidative phosphorylation. Therefore, mitoribosomal function is vital to the cellular energy supply. Mitoribosome biogenesis follows distinct molecular pathways that remain poorly understood. Here, we determine the cryo-EM structures of mitoribosomes isolated from human cell lines with either depleted or overexpressed mitoribosome assembly factor GTPBP5, allowing us to capture consecutive steps during mitoribosomal large subunit (mt-LSU) biogenesis. Our structures provide essential insights into the last steps of 16S rRNA folding, methylation and peptidyl transferase centre (PTC) completion, which require the coordinated action of nine assembly factors. We show that mammalian-specific MTERF4 contributes to the folding of 16S rRNA, allowing 16 S rRNA methylation by MRM2, while GTPBP5 and NSUN4 promote fine-tuning rRNA rearrangements leading to PTC formation. Moreover, our data reveal an unexpected involvement of the elongation factor mtEF-Tu in mt-LSU assembly, where mtEF-Tu interacts with GTPBP5, similar to its interaction with tRNA during translational elongation. PubMed: 34135318DOI: 10.1038/s41467-021-23617-8 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.5 Å) |
Structure validation
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