期刊
SCIENCE
卷 326, 期 5953, 页码 688-694出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1179700
关键词
-
资金
- Medical Research Council U. K.
- Wellcome Trust
- Agouron Institute
- Louis-Jeantet Foundation
- Gates-Cambridge scholarship
- Human Frontiers Science Program Organization and Emmanuel College, University of Cambridge
- MRC [MC_U105184332] Funding Source: UKRI
- Medical Research Council [MC_U105184332] Funding Source: researchfish
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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据