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TitleStructure of the large ribosomal subunit from human mitochondria.
Journal, issue, pagesScience, Vol. 346, Issue 6210, Page 718-722, Year 2014
Publish dateNov 7, 2014
AuthorsAlan Brown / Alexey Amunts / Xiao-Chen Bai / Yoichiro Sugimoto / Patricia C Edwards / Garib Murshudov / Sjors H W Scheres / V Ramakrishnan /
PubMed AbstractHuman mitochondrial ribosomes are highly divergent from all other known ribosomes and are specialized to exclusively translate membrane proteins. They are linked with hereditary mitochondrial ...Human mitochondrial ribosomes are highly divergent from all other known ribosomes and are specialized to exclusively translate membrane proteins. They are linked with hereditary mitochondrial diseases and are often the unintended targets of various clinically useful antibiotics. Using single-particle cryogenic electron microscopy, we have determined the structure of its large subunit to 3.4 angstrom resolution, revealing 48 proteins, 21 of which are specific to mitochondria. The structure unveils an adaptation of the exit tunnel for hydrophobic nascent peptides, extensive remodeling of the central protuberance, including recruitment of mitochondrial valine transfer RNA (tRNA(Val)) to play an integral structural role, and changes in the tRNA binding sites related to the unusual characteristics of mitochondrial tRNAs.
External linksScience / PubMed:25278503 / PubMed Central
MethodsEM (single particle)
Resolution3.4 Å
Structure data

2762

3j7y

EMDB-2762: Electron cryo-microscopy of human mitochondrial large ribosomal subunit
PDB-3j7y: Structure of the large ribosomal subunit from human mitochondria
Method: EM (single particle) / Resolution: 3.4 Å

Chemicals

ChemComp-A:
ADENOSINE-5'-MONOPHOSPHATE / Adenosine monophosphate

ChemComp-MG:
Unknown entry

ChemComp-ZN:
Unknown entry

Source
  • homo sapiens (human)
KeywordsRIBOSOME / mitochondria / large subunit / rRNA / tRNA

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