8OIR
55S human mitochondrial ribosome with mtRF1 and P-site tRNA
This is a non-PDB format compatible entry.
Summary for 8OIR
Entry DOI | 10.2210/pdb8oir/pdb |
EMDB information | 16894 16895 16896 16897 16898 16899 |
Descriptor | 39S ribosomal protein L12, mitochondrial, 39S ribosomal protein L47, mitochondrial, 39S ribosomal protein L30, mitochondrial, ... (98 entities in total) |
Functional Keywords | human mitochondrial ribosome, release factor mtrf1, non-canonical stop codon, ribosome |
Biological source | Homo sapiens (human) More |
Total number of polymer chains | 94 |
Total formula weight | 3149501.82 |
Authors | Saurer, M.,Leibundgut, M.,Scaiola, A.,Schoenhut, T.,Ban, N. (deposition date: 2023-03-23, release date: 2023-06-14, Last modification date: 2024-06-26) |
Primary citation | Saurer, M.,Leibundgut, M.,Nadimpalli, H.P.,Scaiola, A.,Schonhut, T.,Lee, R.G.,Siira, S.J.,Rackham, O.,Dreos, R.,Lenarcic, T.,Kummer, E.,Gatfield, D.,Filipovska, A.,Ban, N. Molecular basis of translation termination at noncanonical stop codons in human mitochondria. Science, 380:531-536, 2023 Cited by PubMed Abstract: The genetic code that specifies the identity of amino acids incorporated into proteins during protein synthesis is almost universally conserved. Mitochondrial genomes feature deviations from the standard genetic code, including the reassignment of two arginine codons to stop codons. The protein required for translation termination at these noncanonical stop codons to release the newly synthesized polypeptides is not currently known. In this study, we used gene editing and ribosomal profiling in combination with cryo-electron microscopy to establish that mitochondrial release factor 1 (mtRF1) detects noncanonical stop codons in human mitochondria by a previously unknown mechanism of codon recognition. We discovered that binding of mtRF1 to the decoding center of the ribosome stabilizes a highly unusual conformation in the messenger RNA in which the ribosomal RNA participates in specific recognition of the noncanonical stop codons. PubMed: 37141370DOI: 10.1126/science.adf9890 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.1 Å) |
Structure validation
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