6ZSB
Human mitochondrial ribosome in complex with mRNA and P-site tRNA
This is a non-PDB format compatible entry.
Summary for 6ZSB
Entry DOI | 10.2210/pdb6zsb/pdb |
EMDB information | 11392 |
Related PRD ID | PRD_000505 |
Descriptor | 39S ribosomal protein L32, mitochondrial, 39S ribosomal protein L41, mitochondrial, 16S mitochondrial rRNA, ... (91 entities in total) |
Functional Keywords | mitochondria, ribosome, mrna, trna, translation |
Biological source | Homo sapiens (human) More |
Total number of polymer chains | 92 |
Total formula weight | 3042257.04 |
Authors | Aibara, S.,Singh, V.,Modelska, A.,Amunts, A. (deposition date: 2020-07-15, release date: 2020-09-16, Last modification date: 2024-07-10) |
Primary citation | Aibara, S.,Singh, V.,Modelska, A.,Amunts, A. Structural basis of mitochondrial translation. Elife, 9:-, 2020 Cited by PubMed Abstract: Translation of mitochondrial messenger RNA (mt-mRNA) is performed by distinct mitoribosomes comprising at least 36 mitochondria-specific proteins. How these mitoribosomal proteins assist in the binding of mt-mRNA and to what extent they are involved in the translocation of transfer RNA (mt-tRNA) is unclear. To visualize the process of translation in human mitochondria, we report ~3.0 Å resolution structure of the human mitoribosome, including the L7/L12 stalk, and eight structures of its functional complexes with mt-mRNA, mt-tRNAs, recycling factor and additional trans factors. The study reveals a transacting protein module LRPPRC-SLIRP that delivers mt-mRNA to the mitoribosomal small subunit through a dedicated platform formed by the mitochondria-specific protein mS39. Mitoribosomal proteins of the large subunit mL40, mL48, and mL64 coordinate translocation of mt-tRNA. The comparison between those structures shows dynamic interactions between the mitoribosome and its ligands, suggesting a sequential mechanism of conformational changes. PubMed: 32812867DOI: 10.7554/eLife.58362 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (4.5 Å) |
Structure validation
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