Incorporation of aminoacyl-tRNA into the ribosome as seen by cryo-electron microscopy

被引：0
作者：
Mikel Valle
Andrey Zavialov
Wen Li
Scott M Stagg
Jayati Sengupta
Rikke C Nielsen
Poul Nissen
Stephen C Harvey
Måns Ehrenberg
Joachim Frank
机构：
[1] Howard Hughes Medical Institute,Department of Cell and Molecular Biology
[2] Health Research,Department of Molecular Biology
[3] Inc. at the Wadsworth Center,Department of Biomedical Sciences
[4] Empire State Plaza,undefined
[5] Biomedical Center,undefined
[6] Box 596,undefined
[7] Wadsworth Center,undefined
[8] Empire State Plaza,undefined
[9] School of Biology,undefined
[10] Georgia Institute of Technology,undefined
[11] University of Aarhus,undefined
[12] Gustav Wieds vej 10C,undefined
[13] State University of New York at Albany,undefined
[14] Empire State Plaza,undefined
[15] Centro Nacional de Biotecnología,undefined
[16] CSIC,undefined
[17] Universidad Autónoma de Madrid,undefined
[18] Cantoblanco,undefined
来源：
Nature Structural Biology | 2003年 / 10卷
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摘要：
Aminoacyl-tRNAs (aa-tRNAs) are delivered to the ribosome as part of the ternary complex of aa-tRNA, elongation factor Tu (EF-Tu) and GTP. Here, we present a cryo-electron microscopy (cryo-EM) study, at a resolution of ∼9 Å, showing that during the incorporation of the aa-tRNA into the 70S ribosome of Escherichia coli, the flexibility of aa-tRNA allows the initial codon recognition and its accommodation into the ribosomal A site. In addition, a conformational change observed in the GTPase-associated center (GAC) of the ribosomal 50S subunit may provide the mechanism by which the ribosome promotes a relative movement of the aa-tRNA with respect to EF-Tu. This relative rearrangement seems to facilitate codon recognition by the incoming aa-tRNA, and to provide the codon-anticodon recognition-dependent signal for the GTPase activity of EF-Tu. From these new findings we propose a mechanism that can explain the sequence of events during the decoding of mRNA on the ribosome.
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页码：899 / 906
页数：7
相关论文
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