5ur5

PYR1 bound to the rationally designed agonist 4m

spinqualitylabelsall models 5ur5, resolution 1.93Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ur5 is a 1 chain structure with sequence from Arath. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 8KP, GOL, SO4 Related: 5ur4, 5ur6 Gene: PYR1, ABIP6, RCAR11, At4g17870, T6K21.50 (ARATH) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PYR1_ARATH] Receptor for abscisic acid (ABA) required for ABA-mediated responses such as stomatal closure and germination inhibition. Inhibits the activity of group-A protein phosphatases type 2C (PP2Cs) when activated by ABA. Publication Abstract from PubMed Increasing drought and diminishing freshwater supplies have stimulated interest in developing small molecules that can be used to control transpiration. Receptors for the plant hormone abscisic acid (ABA) have emerged as key targets for this application, because ABA controls the apertures of stomata, which in turn regulate transpiration. Here, we describe the rational design of cyanabactin, an ABA receptor agonist that preferentially activates Pyrabactin Resistance 1 (PYR1) with low nanomolar potency. A 1.63 A X-ray crystallographic structure of cyanabactin in complex with PYR1 illustrates that cyanabactin's arylnitrile mimics ABA's cyclohexenone oxygen and engages the tryptophan lock, a key component required to stabilize activated receptors. Further, its sulfonamide and 4-methylbenzyl substructures mimic ABA's carboxylate and C6 methyl groups, respectively. Isothermal titration calorimetry measurements show that cyanabactin's compact structure provides ready access to high ligand efficiency on a relatively simple scaffold. Cyanabactin treatments reduce Arabidopsis whole-plant stomatal conductance and activate multiple ABA responses, demonstrating that its in vitro potency translates to ABA-like activity in vivo. Genetic analyses show that the effects of cyanabactin, and the previously identified agonist quinabactin, can be abolished by the genetic removal of PYR1 and PYL1, which form subclade A within the dimeric subfamily III receptors. Thus, cyanabactin is a potent and selective agonist with a wide spectrum of ABA-like activities that defines subfamily IIIA receptors as key target sites for manipulating transpiration. A Rationally Designed Agonist Defines Subfamily IIIA Abscisic Acid Receptors As Critical Targets for Manipulating Transpiration.,Vaidya AS, Peterson FC, Yarmolinsky D, Merilo E, Verstraeten I, Park SY, Elzinga D, Kaundal A, Helander J, Lozano-Juste J, Otani M, Wu K, Jensen DR, Kollist H, Volkman BF, Cutler SR ACS Chem Biol. 2017 Nov 17;12(11):2842-2848. doi: 10.1021/acschembio.7b00650., Epub 2017 Oct 18. PMID:28949512 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Abscisic acid receptor 3D structures

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