Fig. 2: Structure of AMPylated GlnA - hinT H101N complex reveals amino acids at the binding interface. | Nature Communications

Fig. 2: Structure of AMPylated GlnA - hinT H101N complex reveals amino acids at the binding interface.

From: A repurposed AMP binding domain reveals mitochondrial protein AMPylation as a regulator of cellular metabolism

Fig. 2

A Cryo-EM density map representation of the GlnA-hinT H101N complex. The dodecamer GlnA is in blue and the dimeric hinT H101N is in pink. Map obtained from the 3D classification step, for which resolution is not reported by gold-standard FSC. The map is shown at a threshold of 0.023 to better display the density corresponding to hinT. B Enlarged image of cryo-EM density map representation of GlnA-hinT binding interface. AMPylated Tyr-398 present in each of the two GlnA molecules extends into the active site of the dimeric hinT H101N. GlnA subunits colored in dark and light blue. hinT dimer is in magenta and light pink. Map resolution 3.5 Å. C Zoomed in view of the cryo-EM density map representation of GlnA Tyr398-AMP within the hinT H101N binding pocket. GlnA is colored in blue. hinT is in pink. D Enlarged image of the nucleotide binding pocket of hinT H101N, highlighting the hinT amino acid interactions with AMPylated Tyr398 of GlnA.

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