Fig. 3: Ribosomal protein uL16 collaborates with eIF5B DIV in Met-tRNAiMet A76-Met recognition. | Nature Communications

Fig. 3: Ribosomal protein uL16 collaborates with eIF5B DIV in Met-tRNAiMet A76-Met recognition.

From: Structural basis for the transition from translation initiation to elongation by an 80S-eIF5B complex

Fig. 3

a Overall view of the 80S/Met-tRNAiMet/eIF5B complex in an orientation centered on eIF5B DIV. b A detailed view of the Met-tRNAiMet conformation adopted while simultaneously interacts with the mRNA and eIF5B DIV on the 80S. c A detailed view of eIF5B DIV focused on the acceptor stem region of Met-tRNAiMet. DIV of eIF5B is shown in red as semi-transparent Van der Waals surface, Met-tRNAiMet nucleotides depicted in green with experimental cryo-EM density shown and uL16 residues are in blue with experimental cryo-EM density shown. d DIV of eIF5B and residues 102–110 of uL16 form a hydrophobic cavity where the methionine residue of Met-tRNAiMet is hosted.

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