Structure of the large ribosomal subunit from human mitochondria

Alan Brown, Alexey Amunts, Xiao Chen Bai, Yoichiro Sugimoto, Patricia C. Edwards, Garib Murshudov, Sjors H.W. Scheres, V. Ramakrishnan

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151 Scopus citations

Abstract

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 (tRNAVal) to play an integral structural role, and changes in the tRNA binding sites related to the unusual characteristics of mitochondrial tRNAs.

Original languageEnglish (US)
Pages (from-to)718-722
Number of pages5
JournalScience
Volume346
Issue number6210
DOIs
StatePublished - Nov 7 2014

ASJC Scopus subject areas

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    Brown, A., Amunts, A., Bai, X. C., Sugimoto, Y., Edwards, P. C., Murshudov, G., Scheres, S. H. W., & Ramakrishnan, V. (2014). Structure of the large ribosomal subunit from human mitochondria. Science, 346(6210), 718-722. https://doi.org/10.1126/science.1258026