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3NMT

Crystal structure of pyrabactin bound abscisic acid receptor PYL2 mutant A93F in complex with type 2C protein phosphatase HAB1

Summary for 3NMT
Entry DOI10.2210/pdb3nmt/pdb
Related3KB3 3NMH 3NMN 3NMP 3NMV
DescriptorAbscisic acid receptor PYL2, Protein phosphatase 2C 16, 4-bromo-N-(pyridin-2-ylmethyl)naphthalene-1-sulfonamide, ... (6 entities in total)
Functional Keywordspyl2, pyrabactin, abscisic acid receptor, helix-grip fold, protein binding
Biological sourceArabidopsis thaliana (mouse-ear cress,thale-cress)
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Cellular locationCytoplasm : O80992 Q9CAJ0
Total number of polymer chains2
Total formula weight58540.93
Authors
Zhou, X.E.,Melcher, K.,Ng, L.-M.,Soon, F.-F.,Xu, Y.,Suino-Powell, K.M.,Kovach, A.,Li, J.,Yong, E.-L.,Xu, H.E. (deposition date: 2010-06-22, release date: 2010-08-25, Last modification date: 2023-09-06)
Primary citationMelcher, K.,Xu, Y.,Ng, L.M.,Zhou, X.E.,Soon, F.F.,Chinnusamy, V.,Suino-Powell, K.M.,Kovach, A.,Tham, F.S.,Cutler, S.R.,Li, J.,Yong, E.L.,Zhu, J.K.,Xu, H.E.
Identification and mechanism of ABA receptor antagonism.
Nat.Struct.Mol.Biol., 17:1102-1108, 2010
Cited by
PubMed Abstract: The phytohormone abscisic acid (ABA) functions through a family of fourteen PYR/PYL receptors, which were identified by resistance to pyrabactin, a synthetic inhibitor of seed germination. ABA activates these receptors to inhibit type 2C protein phosphatases, such as ABI1, yet it remains unclear whether these receptors can be antagonized. Here we demonstrate that pyrabactin is an agonist of PYR1 and PYL1 but is unexpectedly an antagonist of PYL2. Crystal structures of the PYL2-pyrabactin and PYL1-pyrabactin-ABI1 complexes reveal the mechanism responsible for receptor-selective activation and inhibition, which enables us to design mutations that convert PYL1 to a pyrabactin-inhibited receptor and PYL2 to a pyrabactin-activated receptor and to identify new pyrabactin-based ABA receptor agonists. Together, our results establish a new concept of ABA receptor antagonism, illustrate its underlying mechanisms and provide a rational framework for discovering novel ABA receptor ligands.
PubMed: 20729862
DOI: 10.1038/nsmb.1887
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.56 Å)
Structure validation

238582

数据于2025-07-09公开中

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