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. 2022 Jun 29;50(13):7669–7679. doi: 10.1093/nar/gkac548

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© The Author(s) 2022. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial License (https://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

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Figure 3. — Structure of the 70S ribosome in complex with CHL, A-site glycyl-tRNA, and P-site fMAC-peptidyl-tRNA. (A, B) 2F_o–F_c electron density map (blue mesh) of the A-site Gly-tRNA^Gly (green with glycine residue in magenta) and the P-site peptidyl-tRNA_i^Met (navy with peptide in crimson) bound to the T. thermophilus 70S ribosome in the presence of CHL (yellow). (C, D) Close-up views of the ribosome-bound CHL, highlighting intercalation of its nitrobenzyl group into the A-site cleft formed by nucleotides A2451 and C2452 of the 23S rRNA (C), and the CH-π interactions with the side chain of Ala2 in the peptidyl-tRNA (D). Note that the side chain of the Ala2 residue of the fMAC tripeptide directly interacts with the ribosome-bound CHL.