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

Author

Listed:
  • Wenxue Wang

    (Ocean University of China
    Qingdao Marine Science and Technology Center)

  • Peng Wang

    (Ocean University of China)

  • Chuanteng Ma

    (Ocean University of China)

  • Kang Li

    (Ocean University of China)

  • Zian Wang

    (Ocean University of China)

  • Yuting Liu

    (Ocean University of China)

  • Lu Wang

    (Ocean University of China)

  • Guojian Zhang

    (Ocean University of China
    Qingdao Marine Science and Technology Center)

  • Qian Che

    (Ocean University of China)

  • Tianjiao Zhu

    (Ocean University of China
    Ocean University of China)

  • Yuzhong Zhang

    (Qingdao Marine Science and Technology Center
    Ocean University of China
    Shandong University)

  • Dehai Li

    (Ocean University of China
    Qingdao Marine Science and Technology Center
    Ocean University of China)

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.

Suggested Citation

  • Wenxue Wang & Peng Wang & Chuanteng Ma & Kang Li & Zian Wang & Yuting Liu & Lu Wang & Guojian Zhang & Qian Che & Tianjiao Zhu & Yuzhong Zhang & Dehai Li, 2025. "Characterization and structural analysis of a versatile aromatic prenyltransferase for imidazole-containing diketopiperazines," Nature Communications, Nature, vol. 16(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-024-55537-8
    DOI: 10.1038/s41467-024-55537-8
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    References listed on IDEAS

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    1. Haibing He & Guangkai Bian & Corey J. Herbst-Gervasoni & Takahiro Mori & Stephen A. Shinsky & Anwei Hou & Xin Mu & Minjian Huang & Shu Cheng & Zixin Deng & David W. Christianson & Ikuro Abe & Tiangang, 2020. "Discovery of the cryptic function of terpene cyclases as aromatic prenyltransferases," Nature Communications, Nature, vol. 11(1), pages 1-13, December.
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