3RT2

Crystal structure of apo-PYL10

Summary for 3RT2

• Entry DOI: 10.2210/pdb3rt2/pdb
• Related: 3RT0
• Descriptor: Abscisic acid receptor PYL10 (2 entities in total)
• Functional Keywords: pyl10, aba-independent pp2c inhibitor, pp2cs, abscisic acid, aba receptor, hydrolase inhibitor
• Biological source: Arabidopsis thaliana (thale-cress)
• Cellular location: Cytoplasm (By similarity): Q8H1R0
• Total number of polymer chains: 1
• Total formula weight: 20674.61

Authors

Hao, Q.,Yin, P.,Li, W.,Wang, L.,Yan, C.,Wang, J.,Yan, N. (deposition date: 2011-05-02, release date: 2011-06-22, Last modification date: 2024-10-16)

Primary citation

Hao, Q.,Yin, P.,Li, W.,Wang, L.,Yan, C.,Lin, Z.,Wu, J.Z.,Wang, J.,Yan, S.F.,Yan, N.
The Molecular Basis of ABA-Independent Inhibition of PP2Cs by a Subclass of PYL Proteins
Mol.Cell, 42:662-672, 2011

PubMed Abstract: PYR1/PYL/RCAR proteins (PYLs) are confirmed abscisic acid (ABA) receptors, which inhibit protein phosphatase 2C (PP2C) upon binding to ABA. Arabidopsis thaliana has 14 PYLs, yet their functional distinction remains unclear. Here, we report systematic biochemical characterization of PYLs. A subclass of PYLs, represented by PYL10, inhibited PP2C in the absence of any ligand. Crystal structures of PYL10, both in the free form and in the HAB1 (PP2C)-bound state, revealed the structural basis for its constitutive activity. Structural-guided biochemical analyses revealed that ABA-independent inhibition of PP2C requires the PYLs to exist in a monomeric state. In addition, the residues guarding the entrance to the ligand-binding pocket of these PYLs should be bulky and hydrophobic. Based on these principles, we were able to generate monomeric PYL2 variants that gained constitutive inhibitory effect on PP2Cs. These findings provide an important framework for understanding the complex regulation of ABA signaling by PYL proteins.

PubMed: 21658606
DOI: 10.1016/j.molcel.2011.05.011

Experimental method

X-RAY DIFFRACTION (1.5 Å)