9iia | pdb_00009iia

Crystal structure of the free histidine prenyltransferase FunA

spinqualitylabelsall models 9iia, resolution 2.27Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9iia is a 2 chain structure with sequence from Fusarium tricinctum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.27Å Ligands: MOE, PPV, TOE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A8K0WD55_9HYPO Publication Abstract from PubMed 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 C4-dimethylallylation on l-His. Crystal structure-guided engineering of the prenyl-binding pocket of FunA, a single M181A mutation, successfully converted it into a C4-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. Discovery, Characterization and Engineering of the Free l-Histidine C4-Prenyltransferase.,Chen XW, Liu Z, Dai S, Zou Y J Am Chem Soc. 2024 Aug 28;146(34):23686-23691. doi: 10.1021/jacs.4c08388. Epub , 2024 Aug 14. PMID:39140691 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA