8K9Y
Crystal structure of Arabidopsis thaliana sulfotransferase SOT16 involved in glucosinolate biosynthesis
Summary for 8K9Y
| Entry DOI | 10.2210/pdb8k9y/pdb |
| Descriptor | Cytosolic sulfotransferase 16, ADENOSINE-3'-5'-DIPHOSPHATE, GLYCEROL, ... (6 entities in total) |
| Functional Keywords | sulfotransferase, sulfation, transferase |
| Biological source | Arabidopsis thaliana (thale cress) |
| Total number of polymer chains | 2 |
| Total formula weight | 76838.04 |
| Authors | Iwamoto, Y.,Saito, S.,Teramoto, T.,Kakuta, Y. (deposition date: 2023-08-02, release date: 2023-09-13) |
| Primary citation | Iwamoto, Y.,Saito, S.,Teramoto, T.,Maruyama-Nakashita, A.,Kakuta, Y. Crystal structure of Arabidopsis thaliana sulfotransferase SOT16 involved in glucosinolate biosynthesis. Biochem.Biophys.Res.Commun., 677:149-154, 2023 Cited by PubMed Abstract: Glucosinolates (GSLs), a class of secondary metabolites found in Brassicaceae plants, play important roles in plant defense and contribute distinct flavors and aromas when used as food ingredients. Following tissue damage, GSLs undergo enzymatic hydrolysis to release bioactive volatile compounds. Understanding GSL biosynthesis and enzyme involvement is crucial for improving crop quality and advancing agriculture. Plant sulfotransferases (SOTs) play a key role in the final step of GSL biosynthesis by transferring sulfate groups to the precursor molecules. In the present study, we investigated the enzymatic reaction mechanism and broad substrate specificity of Arabidopsis thaliana sulfotransferase AtSOT16, which is involved in GSL biosynthesis, using crystal structure analysis. Our analysis revealed the specific catalytic residues involved in the sulfate transfer reaction and supported the hypothesis of a concerted acid-base catalytic mechanism. Furthermore, the docking models showed a strong correlation between the substrates with high predicted binding affinities and those experimentally reported to exhibit high activity. These findings provide valuable insights into the enzymatic reaction mechanisms and substrate specificity of GSL biosynthesis. The information obtained in this study may contribute to the development of novel strategies for manipulating GSL synthesis pathways in Brassica plants and has potential agricultural applications. PubMed: 37586213DOI: 10.1016/j.bbrc.2023.08.020 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.82 Å) |
Structure validation
Download full validation report






