9p6k

Colorado Potato Beetle Glutathione S-transferase Sigma Class member 2

spinqualitylabelsall models 9p6k, resolution 2.84Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9p6k is a 4 chain structure with sequence from Leptinotarsa decemlineata. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.84Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A1P8PEX1_LEPDE Publication Abstract from PubMed Understanding the molecular mechanisms underlying insect adaptation is critical for elucidating the evolution of pesticide resistance and improving pest management strategies. While host plant preadaptation has been proposed to facilitate insecticide resistance, direct evidence remains limited. Here, we investigated a sigma-class glutathione S-transferase (GST), LdGSTs2, in the Colorado potato beetle (Leptinotarsa decemlineata), a major agricultural pest. LdGSTs2 is significantly overexpressed in an imidacloprid-resistant strain and induced by host plant allelochemicals. Silencing LdGSTs2 via RNA interference increased susceptibility to imidacloprid, supporting its functional role in resistance. Ligand-binding assays using 8-anilinonaphthalene-1-sulfonic acid (ANS) revealed that LdGSTs2 interacts with a broad range of insecticides and potato-derived phytochemicals. We further solved the 3D crystal structure of LdGSTs2 and performed molecular docking, which identified key residues involved in ligand interactions. These findings demonstrate that LdGSTs2 may contribute to cross-resistance by binding both synthetic and natural xenobiotics, without direct evidence of metabolic detoxification. Our results provide new mechanistic insights into how sigma-class GSTs facilitate adaptation to environmental toxins and highlight a potential molecular link between host plant use and insecticide resistance in specialist herbivores. Crystal structure and ligand binding of a sigma-class glutathione S-transferase associated with cross-resistance in a specialist herbivore.,Moural TW, Hernandez JA, Chen QR, Koirala Bk S, Liu Y, Cofer TM, Zuo IX, Alyokhin A, Wang H, Zhu F Int J Biol Macromol. 2025 Sep;323(Pt 2):147108. doi: , 10.1016/j.ijbiomac.2025.147108. Epub 2025 Aug 25. PMID:40858164 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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