5AJ3

Structure of the small subunit of the mammalian mitoribosome

Summary for 5AJ3

• Entry DOI: 10.2210/pdb5aj3/pdb
• Related: 5AJ4
• EMDB information: 2913
• Descriptor: MITORIBOSOMAL 12S RRNA, MITORIBOSOMAL PROTEIN US12M, MRPS12, MITORIBOSOMAL PROTEIN US14M, MRPS14, ... (40 entities in total)
• Functional Keywords: ribosome, translation, mitochondria, mammalian 55s mitoribosome, mammalian 55s mitochondrial ribosome, 28s small subunit, mrna, trna, decoding center, cryo-em, single particle analysis
• Biological source: Sus scrofa (DOMESTIC PIG); More
• Total number of polymer chains: 37
• Total formula weight: 1148327.02

Authors

Greber, B.J.,Bieri, P.,Leibundgut, M.,Leitner, A.,Aebersold, R.,Boehringer, D.,Ban, N. (deposition date: 2015-02-20, release date: 2015-04-22, Last modification date: 2024-10-23)

Primary citation

Greber, B.J.,Bieri, P.,Leibundgut, M.,Leitner, A.,Aebersold, R.,Boehringer, D.,Ban, N.
Ribosome. The complete structure of the 55S mammalian mitochondrial ribosome.
Science, 348:303-308, 2015

PubMed Abstract: Mammalian mitochondrial ribosomes (mitoribosomes) synthesize mitochondrially encoded membrane proteins that are critical for mitochondrial function. Here we present the complete atomic structure of the porcine 55S mitoribosome at 3.8 angstrom resolution by cryo-electron microscopy and chemical cross-linking/mass spectrometry. The structure of the 28S subunit in the complex was resolved at 3.6 angstrom resolution by focused alignment, which allowed building of a detailed atomic structure including all of its 15 mitoribosomal-specific proteins. The structure reveals the intersubunit contacts in the 55S mitoribosome, the molecular architecture of the mitoribosomal messenger RNA (mRNA) binding channel and its interaction with transfer RNAs, and provides insight into the highly specialized mechanism of mRNA recruitment to the 28S subunit. Furthermore, the structure contributes to a mechanistic understanding of aminoglycoside ototoxicity.

PubMed: 25837512
DOI: 10.1126/science.aaa3872

Experimental method

ELECTRON MICROSCOPY (3.6 Å)