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7ODT

State C of the human mitoribosomal large subunit assembly intermediate

This is a non-PDB format compatible entry.
Summary for 7ODT
Entry DOI10.2210/pdb7odt/pdb
EMDB information12847
DescriptorMitochondrial ribosome-associated GTPase 2, 39S ribosomal protein L35, mitochondrial, 39S ribosomal protein L36, mitochondrial, ... (65 entities in total)
Functional Keywordsmitoribosome, assembly intermediate, large subunit, lsu, mt-lsu, ribosome
Biological sourceHomo sapiens (Human)
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Total number of polymer chains58
Total formula weight1928841.04
Authors
Lenarcic, T.,Jaskolowski, M.,Leibundgut, M.,Scaiola, A.,Schoenhut, T.,Saurer, M.,Lee, R.G.,Rackham, O.,Filipovska, A.,Ban, N. (deposition date: 2021-04-30, release date: 2021-06-23, Last modification date: 2023-11-15)
Primary citationLenarcic, T.,Jaskolowski, M.,Leibundgut, M.,Scaiola, A.,Schonhut, T.,Saurer, M.,Lee, R.G.,Rackham, O.,Filipovska, A.,Ban, N.
Stepwise maturation of the peptidyl transferase region of human mitoribosomes.
Nat Commun, 12:3671-3671, 2021
Cited by
PubMed Abstract: Mitochondrial ribosomes are specialized for the synthesis of membrane proteins responsible for oxidative phosphorylation. Mammalian mitoribosomes have diverged considerably from the ancestral bacterial ribosomes and feature dramatically reduced ribosomal RNAs. The structural basis of the mammalian mitochondrial ribosome assembly is currently not well understood. Here we present eight distinct assembly intermediates of the human large mitoribosomal subunit involving seven assembly factors. We discover that the NSUN4-MTERF4 dimer plays a critical role in the process by stabilizing the 16S rRNA in a conformation that exposes the functionally important regions of rRNA for modification by the MRM2 methyltransferase and quality control interactions with the conserved mitochondrial GTPase MTG2 that contacts the sarcin-ricin loop and the immature active site. The successive action of these factors leads to the formation of the peptidyl transferase active site of the mitoribosome and the folding of the surrounding rRNA regions responsible for interactions with tRNAs and the small ribosomal subunit.
PubMed: 34135320
DOI: 10.1038/s41467-021-23811-8
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.1 Å)
Structure validation

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