Fig. 5: Comparison of the active residues involved in substrate binding in three ternary complexes of AuraA. | Nature Communications

Fig. 5: Comparison of the active residues involved in substrate binding in three ternary complexes of AuraA.

From: Characterization and structural analysis of a versatile aromatic prenyltransferase for imidazole-containing diketopiperazines

Fig. 5

a The residues for the binding of the diphosphate group in AuraA-DMSPP-2 (green) and AuraA-DMSPP-3 (salmon) complexes. b The residues for maintaining tyrosine shielding in AuraA-DMSPP-2/3 complexes. c The residues for interacting with the valine side chains of acceptors in AuraA-DMSPP-2/3 complexes. d The residues for orienting the imidazole moiety of acceptors in AuraA-DMSPP-2/3 complexes. The structures of prenyl donors and acceptors in AuraA-DMSPP-2 and AuraA-DMSPP-3 are represented by lightmagenta and cyan sticks, respectively. R118 and Y354 exhibit significantly different conformations in the AuraA-DMSPP-2 and AuraA-DMSPP-3 structures, marked separately in purpleblue (a, b). The dashed line, colored with gray40, indicates a strong noncovalent bond interaction between two atoms. e The distance between the prenyl acceptors and donors in the AuraA-DMSPP-2 and AuraA-DMSPP-3 structures. These two substrate-binding modes effectively elucidate the reasons behind the formation of products with distinct chemoselectivity. f The residues responsible for maintaining tyrosine shielding within the AuraA-Y207A-DMSPP Cryo-EM structure. Y280 exhibits a significantly different conformation in the AuraA-Y207A-DMSPP structure, marked separately in purpleblue. g Molecular docking of substrate 3 into AuraA-Y207A-DMSPP structure.

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