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. 2021 Dec 1;600(7889):543–546. doi: 10.1038/s41586-021-04131-9

Fig. 1. The translocation-intermediate state of the eukaryotic 80S ribosome with eEF2–GMPPCP, mRNA and tRNAs,, showing diphthamide of eEF2 is involved in stabilizing codon–anticodon interactions early in translocation.

Fig. 1

a, Overview of the translocation-intermediate complex with two tRNAs trapped in chimeric hybrid ap/P and pe/E states. b, Close-up view of ap/P and pe/E tRNA anticodon stem loops in the context of elements of the SSU body and head and domain IV of eEF2. Position of wybutosine (yW) of ap/P tRNAPhe is indicated by the asterisk. c, Position of diphthamide (Diph699) at the conjunction of the AAG anticodon of ap/P tRNAPhe, mRNA codon UUC and decoding adenosines 1755–1756 of helix 44 (h44). d, Stabilization networks around codon–anticodon interactions in the translocation-intermediate complex (left) and the decoding centre of the bacterial ribosome in the cognate classical state13,14 (right). Top, middle and bottom panels depict stabilization around the first, second and third base pairs (BP1–3) of a codon–anticodon duplex, respectively. Conserved adenosines 1755 and 1756 in yeast 18S rRNA correspond to adenosines 1492 and 1493 in 16S rRNA of the bacterial decoding centre. eEF2 is shown in red, mRNA is in orange, chimeric hybrid ap/P tRNA is in green and chimeric hybrid pe/E is in yellow. LSU rRNA and proteins are shown in grey and purple; SSU rRNA and proteins are in cyan and in deep blue. Degrees of SSU body and head rotations are indicated and were obtained by superimposing with the non-rotated 80S ribosome (PDB ID 3J78).