8Y9G
Versatile Aromatic Prenyltransferase auraA in complex with DMSPP and cyclo-(L-Val-DH-His)
This is a non-PDB format compatible entry.
Summary for 8Y9G
| Entry DOI | 10.2210/pdb8y9g/pdb |
| EMDB information | 39079 |
| Descriptor | Versatile Aromatic Prenyltransferase auraA, DIMETHYLALLYL S-THIOLODIPHOSPHATE, (3~{Z},6~{S})-3-(1~{H}-imidazol-4-ylmethylidene)-6-propan-2-yl-piperazine-2,5-dione, ... (4 entities in total) |
| Functional Keywords | prenyltransferase, imidazole-containing diketopiperazines, transferase |
| Biological source | Penicillium |
| Total number of polymer chains | 4 |
| Total formula weight | 187720.38 |
| Authors | |
| 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 Cited by 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: 39747040DOI: 10.1038/s41467-024-55537-8 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.67 Å) |
Structure validation
Download full validation report
