Fig. 2: Structural features of AtEPS1. | Nature Communications

Fig. 2: Structural features of AtEPS1.

From: Mechanistic basis for the emergence of EPS1 as a catalyst in salicylic acid biosynthesis of Brassicaceae

Fig. 2

a The CAG-bound AtEPS1 structure. The N-terminal domain is displayed in salmon, the crossover loop is displayed in slate blue, the dynamic portion of the crossover loop is colored in cyan, the C-terminal domain is displayed in maroon, and the lid loop is colored in purple. |2Fo – Fc| electron density map for the CAG ligand is contoured at 1.5 σ. b Structure of the EPS1 ligand (CAG) and the native substrate (IGA). c The CAG-bound AtEPS1 and the gray superimposed p-coumaroylshikimate-bound AtHCT (PDB: 5KJU). AtEPS1 residues corresponding to the AtHCT catalytic triad and the bulky residues filling the acetyl donor site are individually labeled and colored in salmon. The two catalytic residues of AtHCT are labeled and colored in gray. d Superimposition of the AtEPS1 CAG-bound and apo structures. The apo structure is displayed in bluewhite with the dynamic loops rendered in black. The dynamic loops from both structures are displayed in cartoon putty where the radius of the loops represents relative b-factor. Val355, Ser356, and Val357, annotated in the CAG-bound model, are the only dynamic-loop residues in both structures, within 6 Å distance from CAG.

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