3RT0
Crystal structure of PYL10-HAB1 complex in the absence of abscisic acid (ABA)
Summary for 3RT0
| Entry DOI | 10.2210/pdb3rt0/pdb |
| Related | 3RT2 |
| Descriptor | Protein phosphatase 2C 16, Abscisic acid receptor PYL10, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | pyl10-hab1 binary complex, apo-pyl10 inhibits hab1 dephosphorylation activity, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
| Biological source | Arabidopsis thaliana (thale-cress) More |
| Cellular location | Cytoplasm: Q9CAJ0 Cytoplasm (By similarity): Q8H1R0 |
| Total number of polymer chains | 4 |
| Total formula weight | 116872.14 |
| Authors | |
| 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 Cited by 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: 21658606DOI: 10.1016/j.molcel.2011.05.011 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.113 Å) |
Structure validation
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