7PD3
Structure of the human mitoribosomal large subunit in complex with NSUN4.MTERF4.GTPBP7 and MALSU1.L0R8F8.mt-ACP
This is a non-PDB format compatible entry.
Summary for 7PD3
| Entry DOI | 10.2210/pdb7pd3/pdb |
| EMDB information | 13329 |
| Descriptor | 39S ribosomal protein L32, mitochondrial, 39S ribosomal protein L41, mitochondrial, 16S rRNA, ... (70 entities in total) |
| Functional Keywords | mitochondrial ribosome, large subunit, ribosome biogenesis, gtpase, rrna modification, ribosome |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 60 |
| Total formula weight | 2013690.34 |
| Authors | Chandrasekaran, V.,Desai, N.,Burton, N.O.,Yang, H.,Price, J.,Miska, E.A.,Ramakrishnan, V. (deposition date: 2021-08-04, release date: 2021-11-17) |
| Primary citation | Chandrasekaran, V.,Desai, N.,Burton, N.O.,Yang, H.,Price, J.,Miska, E.A.,Ramakrishnan, V. Visualizing formation of the active site in the mitochondrial ribosome. Elife, 10:-, 2021 Cited by PubMed Abstract: Ribosome assembly is an essential and conserved process that is regulated at each step by specific factors. Using cryo-electron microscopy (cryo-EM), we visualize the formation of the conserved peptidyl transferase center (PTC) of the human mitochondrial ribosome. The conserved GTPase GTPBP7 regulates the correct folding of 16S ribosomal RNA (rRNA) helices and ensures 2'-O-methylation of the PTC base U3039. GTPBP7 binds the RNA methyltransferase NSUN4 and MTERF4, which sequester H68-71 of the 16S rRNA and allow biogenesis factors to access the maturing PTC. Mutations that disrupt binding of their orthologs to the large subunit potently activate mitochondrial stress and cause viability, development, and sterility defects. Next-generation RNA sequencing reveals widespread gene expression changes in these mutant animals that are indicative of mitochondrial stress response activation. We also answer the long-standing question of why NSUN4, but not its enzymatic activity, is indispensable for mitochondrial protein synthesis. PubMed: 34609277DOI: 10.7554/eLife.68806 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.4 Å) |
Structure validation
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