Journal
NATURE STRUCTURAL BIOLOGY
Volume 10, Issue 11, Pages 899-906Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsb1003
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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 similar to9 Angstrom, 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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