9IIA
Crystal structure of the free histidine prenyltransferase FunA
Summary for 9IIA
| Entry DOI | 10.2210/pdb9iia/pdb |
| Descriptor | Dimethylallyl tryptophan synthase GliD1, PYROPHOSPHATE, 2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXYL, ... (5 entities in total) |
| Functional Keywords | free histidine prenyltransferase funa, transferase |
| Biological source | Fusarium tricinctum |
| Total number of polymer chains | 2 |
| Total formula weight | 99377.30 |
| Authors | |
| Primary citation | Chen, X.W.,Liu, Z.,Dai, S.,Zou, Y. Discovery, Characterization and Engineering of the Free l-Histidine C4 -Prenyltransferase. J.Am.Chem.Soc., 146:23686-23691, 2024 Cited by PubMed Abstract: Prenylation of amino acids is a critical step for synthesizing building blocks of prenylated alkaloid family natural products, where the corresponding prenyltransferase that catalyzes prenylation on free l-histidine (l-His) has not yet been identified. Here, we first discovered and characterized a prenyltransferase FunA from the antifungal agent fungerin pathway that efficiently performs -dimethylallylation on l-His. Crystal structure-guided engineering of the prenyl-binding pocket of FunA, a single M181A mutation, successfully converted it into a -geranyltransferase. Furthermore, FunA and its variant FunA-M181A show broad substrate promiscuity toward substrates that vary in substituents of the imidazole ring. Our work furthers our knowledge of free amino acid prenyltransferase and expands the arsenal of alkylation biocatalysts for imidazole-containing small molecules. PubMed: 39140691DOI: 10.1021/jacs.4c08388 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.27 Å) |
Structure validation
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