9JHX

Versatile Aromatic Prenyltransferase auraA mutant-Y207A in complex with DMSPP

This is a non-PDB format compatible entry.

Summary for 9JHX

• Entry DOI: 10.2210/pdb9jhx/pdb
• EMDB information: 61491
• Descriptor: Versatile Aromatic Prenyltransferase auraA, DIMETHYLALLYL S-THIOLODIPHOSPHATE (2 entities in total)
• Functional Keywords: prenyltransferase, imidazole-containing diketopiperazines, transferase
• Biological source: Penicillium solitum
• Total number of polymer chains: 4
• Total formula weight: 196582.51

Authors

Li, D.,Zhang, Y.,Wang, W.,Wang, P. (deposition date: 2024-09-10, release date: 2025-02-05)

Primary citation

Wang, W.,Wang, P.,Ma, C.,Li, K.,Wang, Z.,Liu, Y.,Wang, L.,Zhang, G.,Che, Q.,Zhu, T.,Zhang, Y.,Li, D.
Characterization and structural analysis of a versatile aromatic prenyltransferase for imidazole-containing diketopiperazines.
Nat Commun, 16:144-144, 2025

PubMed 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.

PubMed: 39747040
DOI: 10.1038/s41467-024-55537-8

Experimental method

ELECTRON MICROSCOPY (2.86 Å)