8EY0
Structure of an orthogonal PYR1*:HAB1* chemical-induced dimerization module in complex with mandipropamid
Summary for 8EY0
| Entry DOI | 10.2210/pdb8ey0/pdb |
| Descriptor | Protein phosphatase 2C 16, Abscisic acid receptor PYR1, GLYCEROL, ... (5 entities in total) |
| Functional Keywords | pyr/pyl/rcar, pyr1, hab1, hormone receptor, plant protein, biosensor |
| Biological source | Arabidopsis thaliana (thale cress) More |
| Total number of polymer chains | 2 |
| Total formula weight | 58111.59 |
| Authors | Park, S.-Y.,Volkman, B.F.,Cutler, S.R.,Peterson, F.C. (deposition date: 2022-10-26, release date: 2023-11-08, Last modification date: 2024-01-10) |
| Primary citation | Park, S.Y.,Qiu, J.,Wei, S.,Peterson, F.C.,Beltran, J.,Medina-Cucurella, A.V.,Vaidya, A.S.,Xing, Z.,Volkman, B.F.,Nusinow, D.A.,Whitehead, T.A.,Wheeldon, I.,Cutler, S.R. An orthogonalized PYR1-based CID module with reprogrammable ligand-binding specificity. Nat.Chem.Biol., 20:103-110, 2024 Cited by PubMed Abstract: Plants sense abscisic acid (ABA) using chemical-induced dimerization (CID) modules, including the receptor PYR1 and HAB1, a phosphatase inhibited by ligand-activated PYR1. This system is unique because of the relative ease with which ligand recognition can be reprogrammed. To expand the PYR1 system, we designed an orthogonal '*' module, which harbors a dimer interface salt bridge; X-ray crystallographic, biochemical and in vivo analyses confirm its orthogonality. We used this module to create PYR1*/HAB1* and PYR1*/HAB1*, which possess nanomolar sensitivities to their activating ligands mandipropamid and azinphos-ethyl. Experiments in Arabidopsis thaliana and Saccharomyces cerevisiae demonstrate the sensitive detection of banned organophosphate contaminants using living biosensors and the construction of multi-input/output genetic circuits. Our new modules enable ligand-programmable multi-channel CID systems for plant and eukaryotic synthetic biology that can empower new plant-based and microbe-based sensing modalities. PubMed: 37872402DOI: 10.1038/s41589-023-01447-7 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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