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| Natura: | Artículo científico |
| Lingua: | en |
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Nature communications
2025
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| Soggetti: | |
| Accesso online: | https://pubmed.ncbi.nlm.nih.gov/39747040/ |
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| _version_ | 1868266260631912450 |
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| author | Wang, Wenxue Wang, Peng Ma, Chuanteng Li, Kang Wang, Zian Liu, Yuting Wang, Lu Zhang, Guojian Che, Qian Zhu, Tianjiao Zhang, Yuzhong Li, Dehai |
| author_facet | Wang, Wenxue Wang, Peng Ma, Chuanteng Li, Kang Wang, Zian Liu, Yuting Wang, Lu Zhang, Guojian Che, Qian Zhu, Tianjiao Zhang, Yuzhong Li, Dehai Wang, Wenxue Wang, Peng Ma, Chuanteng Li, Kang Wang, Zian Liu, Yuting Wang, Lu Zhang, Guojian Che, Qian Zhu, Tianjiao Zhang, Yuzhong Li, Dehai |
| collection | PubMed - marine biology |
| contents | Characterization and structural analysis of a versatile aromatic prenyltransferase for imidazole-containing diketopiperazines. Wang, Wenxue Wang, Peng Ma, Chuanteng Li, Kang Wang, Zian Liu, Yuting Wang, Lu Zhang, Guojian Che, Qian Zhu, Tianjiao Zhang, Yuzhong Li, Dehai Imidazoles Dimethylallyltranstransferase Cryoelectron Microscopy Diketopiperazines Prenylation Substrate Specificity Mutation Bacterial Proteins Models, Molecular Streptomyces 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. |
| format | Artículo científico |
| id | pubmed_39747040 |
| institution | PubMed |
| language | en |
| publishDate | 2025 |
| publisher | Nature communications |
| record_format | pubmed |
| spellingShingle | Characterization and structural analysis of a versatile aromatic prenyltransferase for imidazole-containing diketopiperazines. Wang, Wenxue Wang, Peng Ma, Chuanteng Li, Kang Wang, Zian Liu, Yuting Wang, Lu Zhang, Guojian Che, Qian Zhu, Tianjiao Zhang, Yuzhong Li, Dehai Imidazoles Dimethylallyltranstransferase Cryoelectron Microscopy Diketopiperazines Prenylation Substrate Specificity Mutation Bacterial Proteins Models, Molecular Streptomyces Characterization and structural analysis of a versatile aromatic prenyltransferase for imidazole-containing diketopiperazines. Wang, Wenxue Wang, Peng Ma, Chuanteng Li, Kang Wang, Zian Liu, Yuting Wang, Lu Zhang, Guojian Che, Qian Zhu, Tianjiao Zhang, Yuzhong Li, Dehai Imidazoles Dimethylallyltranstransferase Cryoelectron Microscopy Diketopiperazines Prenylation Substrate Specificity Mutation Bacterial Proteins Models, Molecular Streptomyces 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. |
| title | Characterization and structural analysis of a versatile aromatic prenyltransferase for imidazole-containing diketopiperazines. |
| topic | Imidazoles Dimethylallyltranstransferase Cryoelectron Microscopy Diketopiperazines Prenylation Substrate Specificity Mutation Bacterial Proteins Models, Molecular Streptomyces |
| url | https://pubmed.ncbi.nlm.nih.gov/39747040/ |