What recent ribosome structures have revealed about the mechanism of translation

被引:510
作者
Schmeing, T. Martin [1 ]
Ramakrishnan, V. [1 ]
机构
[1] MRC, Mol Biol Lab, Cambridge CB2 0QH, England
基金
英国惠康基金; 英国医学研究理事会;
关键词
PEPTIDE-BOND FORMATION; ELONGATION-FACTOR-G; AMINOACYL-TRANSFER-RNA; COLI 70S RIBOSOME; SUBSTRATE-ASSISTED CATALYSIS; STOP CODON RECOGNITION; SITE TRANSFER-RNA; FACTOR EF-TU; ESCHERICHIA-COLI; CRYSTAL-STRUCTURE;
D O I
10.1038/nature08403
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
The high-resolution structures of ribosomal subunits published in 2000 have revolutionized the field of protein translation. They facilitated the determination and interpretation of functional complexes of the ribosome by crystallography and electron microscopy. Knowledge of the precise positions of residues in the ribosome in various states has facilitated increasingly sophisticated biochemical and genetic experiments, as well as the use of new methods such as single-molecule kinetics. In this review, we discuss how the interaction between structural and functional studies over the last decade has led to a deeper understanding of the complex mechanisms underlying translation.
引用
收藏
页码:1234 / 1242
页数:9
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