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7OG4

Human mitochondrial ribosome in complex with P/E-tRNA

This is a non-PDB format compatible entry.
Replaces:  6ZSF
Summary for 7OG4
Entry DOI10.2210/pdb7og4/pdb
EMDB information12877
Descriptor39S ribosomal protein L32, mitochondrial, 39S ribosomal protein L41, mitochondrial, 16S mitochondrial rRNA, ... (90 entities in total)
Functional Keywordsmitochondria, ribosome, trna, mrna, translation
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains90
Total formula weight3041262.25
Authors
Aibara, S.,Singh, V.,Modelska, A.,Amunts, A. (deposition date: 2021-05-06, release date: 2021-06-23, Last modification date: 2024-07-10)
Primary citationAibara, 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: 32812867
DOI: 10.7554/eLife.58362
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.8 Å)
Structure validation

226707

건을2024-10-30부터공개중

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