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. 2022 Jun 20;40(12):1855–1861. doi: 10.1038/s41587-022-01364-5

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© The Author(s) 2022

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Extended Data Fig. 3 — Diverse H-bond acceptors can stabilize activated PYR/PYL receptors. Structural comparisons of diverse receptor-ligand complexes with the receptor shown in blue and the complexed PP2C (HAB1) is shown in green. (a) In wild-type complexes, the PYR1/ABA/HAB1 complex is stabilized by a hydrogen-bond network coordinated by a central water molecule conserved across ligand-activated receptor X-ray structures (red). The conserved water stabilizes the ternary complex by making contacts to ABA’s cyclohexenone oxygen and PYR1’s P88 main-chain carbonyl oxygen, which serve as H-bond acceptors, and HAB1’s TRP385 indole HN and PYR1’s ARG116 main-chain NH, which serve as H-donors (PDB 3QN1). (b) In the engineered PYL2^WIN receptor, WIN 55,212’s naphthoylindole carbonyl oxygen interacts with the conserved water molecule to engage the TRP-lock, mimicking ABA’s carbonyl oxygen. (c) In the engineered PYR1^MANDI receptor, mandipropamid’s aryl-alkyl ether oxygens stabilizes the PYR1^MANDI/mandipropamid/HAB1 complex via two bound waters that interact with ether oxygens (PDB 4WVO). (d) The rationally designed agonist cyanabactin stabilizes activated PYR1 via an arylnitrile H-bond acceptor that interacts with the conserved water (PDB 5UR6). (e, f) The agonist pyrabactin (with a weak C-Br H-bond acceptor) does not make appreciable contacts with bound water either in homologous PYL1 receptor nor in the engineered PYL2A393F. (e shows PDB ID 3NMT, native PYL1, PDB ID 3NMN is shown in f).