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7QI5

Human mitochondrial ribosome in complex with mRNA, A/A-, P/P- and E/E-tRNAs at 2.63 A resolution

This is a non-PDB format compatible entry.
Summary for 7QI5
Entry DOI10.2210/pdb7qi5/pdb
EMDB information13981
Descriptor12S mitochondrial rRNA, 28S ribosomal protein S12, mitochondrial, VALINE, ... (101 entities in total)
Functional Keywordsribosome, mitochondrial translation, trna, mrna, 2fe-2s clusters, polyamines, rrna modifications, post-translation modifications, cryo em
Biological sourceHomo sapiens (human)
More
Total number of polymer chains94
Total formula weight3136519.25
Authors
Singh, V.,Itoh, Y.,Amunts, A. (deposition date: 2021-12-14, release date: 2023-07-05, Last modification date: 2024-07-31)
Primary citationSingh, V.,Itoh, Y.,Del'Olio, S.,Hassan, A.,Naschberger, A.,Flygaard, R.K.,Nobe, Y.,Izumikawa, K.,Aibara, S.,Andrell, J.,Whitford, P.C.,Barrientos, A.,Taoka, M.,Amunts, A.
Mitoribosome structure with cofactors and modifications reveals mechanism of ligand binding and interactions with L1 stalk.
Nat Commun, 15:4272-4272, 2024
Cited by
PubMed Abstract: The mitoribosome translates mitochondrial mRNAs and regulates energy conversion that is a signature of aerobic life forms. We present a 2.2 Å resolution structure of human mitoribosome together with validated mitoribosomal RNA (rRNA) modifications, including aminoacylated CP-tRNA. The structure shows how mitoribosomal proteins stabilise binding of mRNA and tRNA helping to align it in the decoding center, whereas the GDP-bound mS29 stabilizes intersubunit communication. Comparison between different states, with respect to tRNA position, allowed us to characterize a non-canonical L1 stalk, and molecular dynamics simulations revealed how it facilitates tRNA transitions in a way that does not require interactions with rRNA. We also report functionally important polyamines that are depleted when cells are subjected to an antibiotic treatment. The structural, biochemical, and computational data illuminate the principal functional components of the translation mechanism in mitochondria and provide a description of the structure and function of the human mitoribosome.
PubMed: 38769321
DOI: 10.1038/s41467-024-48163-x
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.63 Å)
Structure validation

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PDB entries from 2024-11-27

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