Fig. 4: The C18 hemisuccinate of RM-A uses its terminal carboxyl group to mimic the phosphate groups of ATP for IleRS binding. | Nature Communications

Fig. 4: The C18 hemisuccinate of RM-A uses its terminal carboxyl group to mimic the phosphate groups of ATP for IleRS binding.

From: Inhibitory mechanism of reveromycin A at the tRNA binding site of a class I synthetase

Fig. 4

a Structural superposition of the T. thermophilus TyrRS ∙ ATP complex (grey, PDB ID: 1H3E) and Bacillus stearothermophilus TrpRS ∙ ATP complex (cyan, PDB ID: 1M83) with the ScIleRS ∙ RM-A ∙ Ile-AMP complex (blue). The backbones of the KMSKS loop form H-bonds with the C4’ carboxyl group of RM-A (indicated as green dashed lines), and they also form similar H-bonds with the β- or γ-phosphates of ATP in ATP-bound TyrRS and TrpRS structures (indicated as grey and cyan dashed lines, respectively). b Structural superposition of the Leishmania major MetRS ∙ Met-AMP ∙ PPi ternary complex (magenta, PDB ID: 3KFL) with the ScIleRS ∙ RM-A ∙ Ile-AMP complex. The H-bonds between the backbones of the KMKSK loop and PPi are indicated as magenta dashed lines.

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