7RKA
Crystal structure analysis of Colorado potato beetle glutathione-S transferase LdGSTu1
Summary for 7RKA
| Entry DOI | 10.2210/pdb7rka/pdb |
| Descriptor | glutathione S-transferase u1, GLUTATHIONE (3 entities in total) |
| Functional Keywords | glutathione s-transferase, gsh, unclassified, colorado potato beetle, imidocloprid resistant, leptinotarsa decemlineata, complex, glutathione, transferase |
| Biological source | Leptinotarsa decemlineata (Colorado potato beetle, Doryphora decemlineata) |
| Total number of polymer chains | 2 |
| Total formula weight | 53207.78 |
| Authors | Moural, T.W.,Zhu, F. (deposition date: 2021-07-22, release date: 2022-07-06, Last modification date: 2023-10-18) |
| Primary citation | Liu, Y.,Moural, T.,Koirala B K, S.,Hernandez, J.,Shen, Z.,Alyokhin, A.,Zhu, F. Structural and Functional Characterization of One Unclassified Glutathione S-Transferase in Xenobiotic Adaptation of Leptinotarsa decemlineata. Int J Mol Sci, 22:-, 2021 Cited by PubMed Abstract: Arthropod Glutathione S-transferases (GSTs) constitute a large family of multifunctional enzymes that are mainly associated with xenobiotic or stress adaptation. GST-mediated xenobiotic adaptation takes place through direct metabolism or sequestration of xenobiotics, and/or indirectly by providing protection against oxidative stress induced by xenobiotic exposure. To date, the roles of GSTs in xenobiotic adaptation in the Colorado potato beetle (CPB), a notorious agricultural pest of plants within Solanaceae, have not been well studied. Here, we functionally expressed and characterized an unclassified-class GST, LdGSTu1. The three-dimensional structure of the LdGSTu1 was solved with a resolution up to 1.8 Å by X-ray crystallography. The signature motif VSDGPPSL was identified in the "G-site", and it contains the catalytically active residue Ser14. Recombinant LdGSTu1 was used to determine enzyme activity and kinetic parameters using 1-chloro-2, 4-dinitrobenzene (CDNB), GSH, p-nitrophenyl acetate (PNA) as substrates. The enzyme kinetic parameters and enzyme-substrate interaction studies demonstrated that LdGSTu1 could catalyze the conjugation of GSH to both CDNB and PNA, with a higher turnover number for CDNB than PNA. The LdGSTu1 enzyme inhibition assays demonstrated that the enzymatic conjugation of GSH to CDNB was inhibited by multiple pesticides, suggesting a potential function of LdGSTu1 in xenobiotic adaptation. PubMed: 34769352DOI: 10.3390/ijms222111921 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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