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8AYA

X-RAY CRYSTAL STRUCTURE OF THE CsPYL1-A10-HAB1 TERNARY COMPLEX

Summary for 8AYA
Entry DOI10.2210/pdb8aya/pdb
DescriptorAbscisic acid receptor PYL1, Protein phosphatase 2C 16, Quinabactin, ... (7 entities in total)
Functional Keywordscspyl1, hab1, phosphatase aba receptor inhibitor complex, plant protein
Biological sourceCitrus sinensis (sweet orange)
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Total number of polymer chains2
Total formula weight61028.87
Authors
Infantes, L.,Albert, A. (deposition date: 2022-09-02, release date: 2023-03-22, Last modification date: 2024-02-07)
Primary citationLozano-Juste, J.,Infantes, L.,Garcia-Maquilon, I.,Ruiz-Partida, R.,Merilo, E.,Benavente, J.L.,Velazquez-Campoy, A.,Coego, A.,Bono, M.,Forment, J.,Pampin, B.,Destito, P.,Monteiro, A.,Rodriguez, R.,Cruces, J.,Rodriguez, P.L.,Albert, A.
Structure-guided engineering of a receptor-agonist pair for inducible activation of the ABA adaptive response to drought.
Sci Adv, 9:eade9948-eade9948, 2023
Cited by
PubMed Abstract: Strategies to activate abscisic acid (ABA) receptors and boost ABA signaling by small molecules that act as ABA receptor agonists are promising biotechnological tools to enhance plant drought tolerance. Protein structures of crop ABA receptors might require modifications to improve recognition of chemical ligands, which in turn can be optimized by structural information. Through structure-based targeted design, we have combined chemical and genetic approaches to generate an ABA receptor agonist molecule (iSB09) and engineer a CsPYL1 ABA receptor, named CsPYL1, which efficiently binds iSB09. This optimized receptor-agonist pair leads to activation of ABA signaling and marked drought tolerance. No constitutive activation of ABA signaling and hence growth penalty was observed in transformed plants. Therefore, conditional and efficient activation of ABA signaling was achieved through a chemical-genetic orthogonal approach based on iterative cycles of ligand and receptor optimization driven by the structure of ternary receptor-ligand-phosphatase complexes.
PubMed: 36897942
DOI: 10.1126/sciadv.ade9948
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.742 Å)
Structure validation

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