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3J9M

Structure of the human mitochondrial ribosome (class 1)

This is a non-PDB format compatible entry.
Summary for 3J9M
Entry DOI10.2210/pdb3j9m/pdb
EMDB information2876 2880 2881
Descriptor16S rRNA, uL14m, uL15m, ... (88 entities in total)
Functional Keywordsmitochondria, translation, ribosome
Biological sourceHomo sapiens (human)
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Total number of polymer chains85
Total formula weight2865036.65
Authors
Amunts, A.,Brown, A.,Toots, J.,Scheres, S.H.,Ramakrishnan, V. (deposition date: 2015-02-08, release date: 2015-04-15, Last modification date: 2024-11-06)
Primary citationAmunts, A.,Brown, A.,Toots, J.,Scheres, S.H.,Ramakrishnan, V.
Ribosome. The structure of the human mitochondrial ribosome.
Science, 348:95-98, 2015
Cited by
PubMed Abstract: The highly divergent ribosomes of human mitochondria (mitoribosomes) synthesize 13 essential proteins of oxidative phosphorylation complexes. We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by means of single-particle electron cryogenic microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three ribosomal RNA molecules. The head domain of the small subunit, particularly the messenger (mRNA) channel, is highly remodeled. Many intersubunit bridges are specific to the mitoribosome, which adopts conformations involving ratcheting or rolling of the small subunit that are distinct from those seen in bacteria or eukaryotes. An intrinsic guanosine triphosphatase mediates a contact between the head and central protuberance. The structure provides a reference for analysis of mutations that cause severe pathologies and for future drug design.
PubMed: 25838379
DOI: 10.1126/science.aaa1193
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.5 Å)
Structure validation

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