Structure of the large ribosomal subunit from human mitochondria

Item Type:	Article
Title:	Structure of the large ribosomal subunit from human mitochondria
Creators Name:	Brown, A. and Amunts, A. and Bai, X.C. and Sugimoto, Y. and Edwards, P.C. and Murshudov, G. and Scheres, S.H.W. and Ramakrishnan, V.
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 (tRNA(Val)) to play an integral structural role, and changes in the tRNA binding sites related to the unusual characteristics of mitochondrial tRNAs.
Keywords:	Binding Sites, Cryoelectron Microscopy, Mitochondria, Mitochondrial Proteins, Mutation, Nucleic Acid Conformation, Protein Conformation, Ribosome Subunits, Val Transfer RNA
Source:	Science
ISSN:	0036-8075
Publisher:	American Association for the Advancement of Science
Volume:	346
Number:	6210
Page Range:	718-722
Date:	7 November 2014
Official Publication:	https://doi.org/10.1126/science.1258026
PubMed:	View item in PubMed

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