3kdj | pdb_00003kdj

Complex structure of (+)-ABA-bound PYL1 and ABI1

spinqualitylabelsall models 3kdj, resolution 1.88Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3kdj is a 2 chain structure with sequence from Arath. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: A8S, MN Related: 3kdh, 3kdi Gene: At5g46790 (ARATH), ABI1, At4g26080, F20B18.190 (ARATH) Activity: Phosphoprotein phosphatase, with EC number 3.1.3.16 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PYL1_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. [P2C56_ARATH] Key component and repressor of the abscisic acid (ABA) signaling pathway that regulates numerous ABA responses, such as stomatal closure, osmotic water permeability of the plasma membrane (Pos), drought-induced resistance and rhizogenesis, response to glucose, high light stress, seed germination and inhibition of vegetative growth. During the stomatal closure regulation, modulates the inward calcium-channel permeability as well as the actin reorganization in guard cells in response to ABA. Involved in the resistance to the bacterial pathogen Pseudomonas syringae pv. tomato. Controls negatively fibrillin expression that is involved in mediating ABA-induced photoprotection. May be involved in ABA content regulation. Plays a role in the Pro accumulation in response to reduced water availability (low water potential). Required for the ABA negative regulation of the ethylene-induced hyponastic growth. Involved in acquired thermotolerance of root growth and seedling survival. Activates/represses SRK2E/OST1 in response to ABA-dependent stimuli, especially in stomata closure regulation involving SLAC1. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Abscisic acid (ABA) is an important phytohormone that regulates plant stress responses. Proteins from the PYR-PYL-RCAR family were recently identified as ABA receptors. Upon binding to ABA, a PYL protein associates with type 2C protein phosphatases (PP2Cs) such as ABI1 and ABI2, inhibiting their activity; the molecular mechanisms by which PYLs mediate ABA signaling remain unknown, however. Here we report three crystal structures: apo-PYL2, (+)-ABA-bound PYL2 and (+)-ABA-bound PYL1 in complex with phosphatase ABI1. Apo-PYL2 contains a pocket surrounded by four highly conserved surface loops. In response to ABA binding, loop CL2 closes onto the pocket, creating a surface that recognizes ABI1. In the ternary complex, the CL2 loop is located near the active site of ABI1, blocking the entry of substrate proteins. Together, our data reveal the mechanisms by which ABA regulates PYL-mediated inhibition of PP2Cs. Structural insights into the mechanism of abscisic acid signaling by PYL proteins.,Yin P, Fan H, Hao Q, Yuan X, Wu D, Pang Y, Yan C, Li W, Wang J, Yan N Nat Struct Mol Biol. 2009 Dec;16(12):1230-6. Epub 2009 Nov 5. PMID:19893533 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Abscisic acid receptor 3D structures Protein phosphatase 3D structures

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