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5WFS

70S ribosome-EF-Tu H84A complex with GTP and near-cognate tRNA (Complex C4)

This is a non-PDB format compatible entry.
Summary for 5WFS
Entry DOI10.2210/pdb5wfs/pdb
Related5WF0 5WFK
EMDB information8826 8828 8829
Descriptor23S rRNA, 50S ribosomal protein L13, 50S ribosomal protein L14, ... (64 entities in total)
Functional Keywordstranslation, gtpase, ribosome
Biological sourceEscherichia coli
More
Total number of polymer chains59
Total formula weight2297549.01
Authors
Fislage, M.,Frank, J. (deposition date: 2017-07-12, release date: 2018-05-02, Last modification date: 2024-03-13)
Primary citationFislage, M.,Zhang, J.,Brown, Z.P.,Mandava, C.S.,Sanyal, S.,Ehrenberg, M.,Frank, J.
Cryo-EM shows stages of initial codon selection on the ribosome by aa-tRNA in ternary complex with GTP and the GTPase-deficient EF-TuH84A.
Nucleic Acids Res., 46:5861-5874, 2018
Cited by
PubMed Abstract: 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 the monitoring 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.
PubMed: 29733411
DOI: 10.1093/nar/gky346
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3 Å)
Structure validation

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건을2024-11-06부터공개중

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