Journal
EMBO JOURNAL
Volume 30, Issue 8, Pages 1497-1507Publisher
WILEY
DOI: 10.1038/emboj.2011.58
Keywords
cryo-EM; ribosome; ternary complex; translation; tRNA incorporation
Categories
Funding
- Spanish Government [RYC-2009-04885]
- Alexander von Humboldt Foundation
- European Molecular Biology Organization
- HHMI
- NIH [R01 GM55440, R37 GM29169, R01 GM059425, P41-RR005969]
- NSF [PHY0822613]
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The structural basis of the tRNA selection process is investigated by cryo-electron microscopy of ribosomes programmed with UGA codons and incubated with ternary complex (TC) containing the near-cognate Trp-tRNA(Trp) in the presence of kirromycin. Going through more than 350 000 images and employing image classification procedures, we find similar to 8% in which the TC is bound to the ribosome. The reconstructed 3D map provides a means to characterize the arrangement of the near-cognate aa-tRNA with respect to elongation factor Tu (EF-Tu) and the ribosome, as well as the domain movements of the ribosome. One of the interesting findings is that near-cognate tRNA's acceptor stem region is flexible and CCA end becomes disordered. The data bring direct structural insights into the induced-fit mechanism of decoding by the ribosome, as the analysis of the interactions between small and large ribosomal subunit, aa-tRNA and EF-Tu and comparison with the cognate case (UGG codon) offers clues on how the conformational signals conveyed to the GTPase differ in the two cases. The EMBO Journal (2011) 30, 1497-1507. doi:10.1038/emboj.2011.58; Published online 4 March 2011 Subject Categories: proteins; structural biology
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