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. 2023 Dec 15;52(2):513–524. doi: 10.1093/nar/gkad1188

Figure 6.

Figure 6.

Mutations to tRNAPyl induce rigidity, conforming these tRNAs to an ideal structure for recognition by MaPylRS. (A) tRNAPyl variants Mm05 and Dh02 were found to be more rigid and have a canonical L-shaped compared to their parent tRNAPyl (Mm and Dh, respectively). (B) Measuring three distances at the proposed Ma tRNAPyl:MaPylRS interface (PDBID:6EZD) revealed the necessary distances required for maximal activity with MaPylRS. Distance 1 is shown to be the major contributor in this recognition.