5ZFG
Crystal structure of a diazinon-metabolizing glutathione S-transferase in the silkworm, Bombyx mori
Summary for 5ZFG
| Entry DOI | 10.2210/pdb5zfg/pdb |
| Descriptor | Glutathione S-transferase, 1,2-ETHANEDIOL, ACETATE ION, ... (4 entities in total) |
| Functional Keywords | lepidoptera, glutathione, glutathione transferase, diazinon, transferase |
| Biological source | Bombyx mori (Silk moth) |
| Total number of polymer chains | 2 |
| Total formula weight | 53763.40 |
| Authors | Yamamoto, K.,Higashiura, A.,Nakagawa, A. (deposition date: 2018-03-06, release date: 2018-09-12, Last modification date: 2024-03-27) |
| Primary citation | Yamamoto, K.,Higashiura, A.,Hirowatari, A.,Yamada, N.,Tsubota, T.,Sezutsu, H.,Nakagawa, A. Characterisation of a diazinon-metabolising glutathione S-transferase in the silkworm Bombyx mori by X-ray crystallography and genome editing analysis. Sci Rep, 8:16835-16835, 2018 Cited by PubMed Abstract: Previously, we found an unclassified glutathione S-transferase 2 (bmGSTu2) in the silkworm Bombyx mori that conjugates glutathione to 1-chloro-2,4-dinitrobenzene and also metabolises diazinon, an organophosphate insecticide. Here, we provide a structural and genome-editing characterisation of the diazinon-metabolising glutathione S-transferase in B. mori. The structure of bmGSTu2 was determined at 1.68 Å by X-ray crystallography. Mutation of putative amino acid residues in the substrate-binding site showed that Pro13, Tyr107, Ile118, Phe119, and Phe211 are crucial for enzymatic function. bmGSTu2 gene disruption resulted in a decrease in median lethal dose values to an organophosphate insecticide and a decrease in acetylcholine levels in silkworms. Taken together, these results indicate that bmGSTu2 could metabolise an organophosphate insecticide. Thus, this study provides insights into the physiological role of bmGSTu2 in silkworms, detoxification of organophosphate insecticides, and drug targets for the development of a novel insecticide. PubMed: 30443011DOI: 10.1038/s41598-018-35207-8 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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