Figure 5: Comparison of TM84 and Leu-AMS bound in LeuRSEc ternary complexes. | Nature Communications

Figure 5: Comparison of TM84 and Leu-AMS bound in LeuRSEc ternary complexes.

From: Plant tumour biocontrol agent employs a tRNA-dependent mechanism to inhibit leucyl-tRNA synthetase

Figure 5

(a) TM84 (pink) binding in the synthetic active site showing interactions with the KMSKS loop (gold) and the terminal tRNA Ade76 (blue). The ribose of the adenosine is in the C2′-endo conformation. Water molecule depicted as a red sphere. (b) Leu-AMS (grey) in its respective ternary complex. The ribose of the adenosine in this structure is in the C2′-exo conformation. (c) Superimposition of the two ligands in their respective ternary complexes.

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