Journal
NUCLEIC ACIDS RESEARCH
Volume 46, Issue 11, Pages 5861-5874Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gky346
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Funding
- Howard Hughes Medical Institute (HHMI)
- National Institutes of Health [R01 GM29169]
- 'Program of Leading Graduate Schools' of the ministry of education, sports, science and technology, Japan
- Swedish Research Council [2013-8778, 2014-4423, 2016-06264, 2017-00230]
- Knut and Alice Wallenberg Foundation [KAW 2011.0081]
- National Institutes of Health
- Swedish Research Council [2017-00230] Funding Source: Swedish Research Council
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The GTPase EF-Tu in ternary complex with GTP and aminoacyl-tRNA (aa-tRNA) promotes rapid and accurate delivery of cognate aa-tRNAs to the ribosomal A site. Here we used cryo-EM to study the molecular origins of the accuracy of ribosome-aided recognition of a cognate ternary complex and the accuracy-amplifying role of themonitoring bases A1492, A1493 and G530 of the 16S rRNA. We used the GTPase-deficient EF-Tu variant H84A with native GTP, rather than non-cleavable GTP analogues, to trap a near-cognate ternary complex in high-resolution ribosomal complexes of varying codon-recognition accuracy. We found that ribosome complexes trapped by GTPase-deficicent ternary complex due to the presence of EF-TuH84A or non-cleavable GTP analogues have very similar structures. We further discuss speed and accuracy of initial aa-tRNA selection in terms of conformational changes of aa-tRNA and stepwise activation of the monitoring bases at the decoding center of the ribosome.
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