The Crystal Structure of the Ribosome Bound to EF-Tu and Aminoacyl-tRNA

被引：414

作者：

Schmeing, T. Martin ^{[1
]}

Voorhees, Rebecca M. ^{[1
]}

Kelley, Ann C. ^{[1
]}

Gao, Yong-Gui ^{[1
]}

Murphy, Frank V., IV ^{[1
]}

Weir, John R. ^{[1
]}

Ramakrishnan, V. ^{[1
]}

机构：

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

来源：

SCIENCE | 2009年 / 326卷 / 5953期

基金：

英国医学研究理事会; 英国惠康基金;

关键词：

ELONGATION-FACTOR TU; GTPASE ACTIVATION; ESCHERICHIA-COLI; ACTIVE-ROLE; CROSS-LINK; SELECTION; HYDROLYSIS; BINDING; COMPLEX; RECOGNITION;

D O I：

10.1126/science.1179700

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 ribosome selects a correct transfer RNA (tRNA) for each amino acid added to the polypeptide chain, as directed by messenger RNA. Aminoacyl-tRNA is delivered to the ribosome by elongation factor Tu (EF-Tu), which hydrolyzes guanosine triphosphate (GTP) and releases tRNA in response to codon recognition. The signaling pathway that leads to GTP hydrolysis upon codon recognition is critical to accurate decoding. Here we present the crystal structure of the ribosome complexed with EF-Tu and aminoacyl-tRNA, refined to 3.6 angstrom resolution. The structure reveals details of the tRNA distortion that allows aminoacyl-tRNA to interact simultaneously with the decoding center of the 30S subunit and EF-Tu at the factor binding site. A series of conformational changes in EF-Tu and aminoacyl-tRNA suggests a communication pathway between the decoding center and the guanosine triphosphatase center of EF-Tu.

引用

页码：688 / 694

页数：7

共 43 条

[1] CRYSTAL-STRUCTURE OF ACTIVE ELONGATION-FACTOR TU REVEALS MAJOR DOMAIN REARRANGEMENTS [J].