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

Bibliographic Details
Title: Characterization and structural analysis of a versatile aromatic prenyltransferase for imidazole-containing diketopiperazines
Authors: Wenxue Wang, Peng Wang, Chuanteng Ma, Kang Li, Zian Wang, Yuting Liu, Lu Wang, Guojian Zhang, Qian Che, Tianjiao Zhu, Yuzhong Zhang, Dehai Li
Source: Nature Communications, Vol 16, Iss 1, Pp 1-10 (2025)
Publisher Information: Nature Portfolio, 2025.
Publication Year: 2025
Collection: LCC:Science
Subject Terms: Science
More Details: Abstract Prenylation 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.
Document Type: article
File Description: electronic resource
Language: English
ISSN: 2041-1723
Relation: https://doaj.org/toc/2041-1723
DOI: 10.1038/s41467-024-55537-8
Access URL: https://doaj.org/article/9038966b01b24f9e8b8b59f603840aca
Accession Number: edsdoj.9038966b01b24f9e8b8b59f603840aca
Database: Directory of Open Access Journals
More Details
ISSN:20411723
DOI:10.1038/s41467-024-55537-8
Published in:Nature Communications
Language:English