6ZS9

Human mitochondrial ribosome in complex with ribosome recycling factor

This is a non-PDB format compatible entry.

Summary for 6ZS9

• Entry DOI: 10.2210/pdb6zs9/pdb
• EMDB information: 11390
• Related PRD ID: PRD_000505
• Descriptor: 39S ribosomal protein L32, mitochondrial, 39S ribosomal protein L41, mitochondrial, 16S rRNA, ... (90 entities in total)
• Functional Keywords: mitochondria, ribosome, mrna, trna, translation
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 91
• Total formula weight: 3025741.37

Authors

Aibara, S.,Singh, V.,Modelska, A.,Amunts, A. (deposition date: 2020-07-15, release date: 2020-10-14, Last modification date: 2024-07-10)

Primary citation

Aibara, S.,Singh, V.,Modelska, A.,Amunts, A.
Structural basis of mitochondrial translation.
Elife, 9:-, 2020

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

Experimental method

ELECTRON MICROSCOPY (4 Å)