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. 2024 Feb 14;626(8001):1125–1132. doi: 10.1038/s41586-024-07041-8

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© The Author(s) 2024

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

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Extended Data Fig. 8 — (a) Cryo-EM maps comparing the binding of Balon and its homologues Msmeg1130 (from M. smegmatis) and Rv2629 (M. tuberculosis) to the A site of bacterial ribosomes. (b) Zoomed-in view illustrating the protein/protein interaction interface for the ribosome-bound complex of Msmeg1130/EF-Tu. (c) Multiple sequence alignment for EF-Tu from T. aquaticus, P. urativorans, M. smegmatis, M. tuberculosis, and E. coli, illustrating the high conservation of the Balon-binding site in EF-Tu from different bacteria. This panel shows that Balon and its mycobacterial homologues Msmeg1130 and Rv2629 recognize the same residues in domain III of EF-Tu that are involved in tRNA-binding (highlighted in green).