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Versatile Aromatic Prenyltransferase auraA for Imidazole-Containing DiketopiperazinesVersatile Aromatic Prenyltransferase auraA for Imidazole-Containing Diketopiperazines
Structural highlights
Publication Abstract from PubMedPrenylation modifications of natural products play essential roles in chemical diversity and bioactivities, but imidazole modification prenyltransferases are not well investigated. Here, we discover a dimethylallyl tryptophan synthase family prenyltransferase, AuraA, that catalyzes the rare dimethylallylation on the imidazole moiety in the biosynthesis of aurantiamine. Biochemical assays validate that AuraA could accept both cyclo-(L-Val-L-His) and cyclo-(L-Val-DH-His) as substrates, while the prenylation modes are completely different, yielding C2-regular and C5-reverse products, respectively. Cryo-electron microscopy analysis of AuraA and its two ternary complex structures reveal two distinct modes for receptor binding, demonstrating a tolerance for altered orientations of highly similar receptors. The mutation experiments further demonstrate the promiscuity of AuraA towards imidazole-C-dimethylallylation. In this work, we also characterize a case of AuraA mutant-catalyzed dimethylallylation of imidazole moiety, offering available structural insights into the utilization and engineering of dimethylallyl tryptophan synthase family prenyltransferases. Characterization and structural analysis of a versatile aromatic prenyltransferase for imidazole-containing diketopiperazines.,Wang W, Wang P, Ma C, Li K, Wang Z, Liu Y, Wang L, Zhang G, Che Q, Zhu T, Zhang Y, Li D Nat Commun. 2025 Jan 2;16(1):144. doi: 10.1038/s41467-024-55537-8. PMID:39747040[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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