4CE4

39S large subunit of the porcine mitochondrial ribosome

Summary for 4CE4

• Entry DOI: 10.2210/pdb4ce4/pdb
• EMDB information: 2490
• Descriptor: MRPL27, 16S Ribosomal RNA, UNASSIGNED RNA, ... (38 entities in total)
• Functional Keywords: ribosome, mammalian mitochondrial ribosome, 39s large ribosomal subunit, translation, ribosomal proteins, rrna, polypeptide exit site, membrane association
• Biological source: SUS SCROFA DOMESTICA (DOMESTIC PIG); More
• Total number of polymer chains: 38
• Total formula weight: 1307235.68

Authors

Greber, B.J.,Boehringer, D.,Leitner, A.,Bieri, P.,Voigts-Hoffmann, F.,Erzberger, J.P.,Leibundgut, M.,Aebersold, R.,Ban, N. (deposition date: 2013-11-08, release date: 2013-12-18, Last modification date: 2024-05-08)

Primary citation

Greber, B.J.,Boehringer, D.,Leitner, A.,Bieri, P.,Voigts-Hoffmann, F.,Erzberger, J.P.,Leibundgut, M.,Aebersold, R.,Ban, N.
Architecture of the Large Subunit of the Mammalian Mitochondrial Ribosome.
Nature, 505:515-, 2014

PubMed Abstract: Mitochondrial ribosomes synthesize a number of highly hydrophobic proteins encoded on the genome of mitochondria, the organelles in eukaryotic cells that are responsible for energy conversion by oxidative phosphorylation. The ribosomes in mammalian mitochondria have undergone massive structural changes throughout their evolution, including ribosomal RNA shortening and acquisition of mitochondria-specific ribosomal proteins. Here we present the three-dimensional structure of the 39S large subunit of the porcine mitochondrial ribosome determined by cryo-electron microscopy at 4.9 Å resolution. The structure, combined with data from chemical crosslinking and mass spectrometry experiments, reveals the unique features of the 39S subunit at near-atomic resolution and provides detailed insight into the architecture of the polypeptide exit site. This region of the mitochondrial ribosome has been considerably remodelled compared to its bacterial counterpart, providing a specialized platform for the synthesis and membrane insertion of the highly hydrophobic protein components of the respiratory chain.

PubMed: 24362565
DOI: 10.1038/NATURE12890

Experimental method

ELECTRON MICROSCOPY (4.9 Å)