Structure of the large ribosomal subunit from human mitochondria | Zendy

Alan Brown | Zendy; Alexey Amunts | Zendy; Xiaochen Bai | Zendy; Yoichiro Sugimoto | Zendy; Patricia C. Edwards | Zendy; Garib N. Murshudov | Zendy; Sjors H. W. Scheres | Zendy; V. Ramakrishnan | Zendy

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Structure of the large ribosomal subunit from human mitochondria

Author(s) -

Alan Brown,

Alexey Amunts,

Xiaochen Bai,

Yoichiro Sugimoto,

Patricia C. Edwards,

Garib N. Murshudov,

Sjors H. W. Scheres,

V. Ramakrishnan

Publication year - 2014

Publication title -

science

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 12.556

H-Index - 1186

eISSN - 1095-9203

pISSN - 0036-8075

DOI - 10.1126/science.1258026

Subject(s) - mitochondrial ribosome , ribosome , mitochondrion , cytoplasm , ribosomal protein , protein subunit , inner mitochondrial membrane , ribosomal rna , biology , biochemistry , microbiology and biotechnology , chemistry , biophysics , rna , gene

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.

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