Structure of the large ribosomal subunit from human mitochondria

被引：235

作者：

Brown, Alan ^{[1
]}

Amunts, Alexey ^{[1
]}

Bai, Xiao-chen ^{[1
]}

Sugimoto, Yoichiro ^{[1
]}

Edwards, Patricia C. ^{[1
]}

Murshudov, Garib ^{[1
]}

Scheres, Sjors H. W. ^{[1
]}

Ramakrishnan, V. ^{[1
]}

机构：

[1] MRC, Mol Biol Lab, Cambridge CB2 0QH, England

来源：

SCIENCE | 2014年 / 346卷 / 6210期

基金：

英国医学研究理事会; 英国惠康基金;

关键词：

ELONGATION-FACTOR-G; CRYO-EM STRUCTURE; TRANSFER-RNA; TRANSLATION; SNAPSHOTS; REVEALS; SEARCH; GENES; STALK; L11;

D O I：

10.1126/science.1258026

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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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页码：718 / 722

页数：5

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