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- Title
Incorporation of aminoacyl-tRNA into the ribosome as seen by cryo-electron microscopy.
- Authors
Valle, Mikel; Zavialov, Andrey; Li, Wen; Stagg, Scott M; Sengupta, Jayati; Nielsen, Rikke C; Nissen, Poul; Harvey, Stephen C; Ehrenberg, Måns; Frank, Joachim
- Abstract
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.
- Subjects
AMINOACYL-tRNA; ELECTRON microscopy; TRANSFER RNA; AMINO acids; MICROSCOPY
- Publication
Nature Structural Biology, 2003, Vol 10, Issue 11, p899
- ISSN
1072-8368
- Publication type
Article
- DOI
10.1038/nsb1003