4DSB
Complex Structure of Abscisic Acid Receptor PYL3 with (+)-ABA in Spacegroup of I 212121 at 2.70A
Summary for 4DSB
Entry DOI | 10.2210/pdb4dsb/pdb |
Related | 3KLX 3OJI 4DS8 4DSC |
Descriptor | Abscisic acid receptor PYL3, (2Z,4E)-5-[(1S)-1-hydroxy-2,6,6-trimethyl-4-oxocyclohex-2-en-1-yl]-3-methylpenta-2,4-dienoic acid (3 entities in total) |
Functional Keywords | abscisic acid receptor, aba, pyl3, hormone receptor |
Biological source | Arabidopsis thaliana (mouse-ear cress) |
Cellular location | Cytoplasm (By similarity): Q9SSM7 |
Total number of polymer chains | 2 |
Total formula weight | 42444.42 |
Authors | |
Primary citation | Zhang, X.,Zhang, Q.,Xin, Q.,Yu, L.,Wang, Z.,Wu, W.,Jiang, L.,Wang, G.,Tian, W.,Deng, Z.,Wang, Y.,Liu, Z.,Long, J.,Gong, Z.,Chen, Z. Complex Structures of the Abscisic Acid Receptor PYL3/RCAR13 Reveal a Unique Regulatory Mechanism Structure, 20:780-790, 2012 Cited by PubMed Abstract: Abscisic acid (ABA) controls many physiological processes and mediates adaptive responses to abiotic stresses. The ABA signaling mechanisms for abscisic acid receptors PYR/PYL/RCAR (PYLs) were reported. However, it remains unclear whether the molecular mechanisms are suitable for other PYLs. Here, complex structures of PYL3 with (+)-ABA, pyrabactin and HAB1 are reported. An unexpected trans-homodimer intermediate observed in the crystal is confirmed in solution. ABA-bound PYL3 greatly promotes the generation of monomeric PYL3, which can excessively increase the efficiency of inhibiting PP2Cs. Structure-guided biochemical experiments show that Ser195 accounts for the key intermediate. Interestingly, pyrabactin binds to PYL3 in a distinct nonproductive mode with gate closure, which sheds light on the design of agonists and antagonists for abscisic acid receptors. According to different conformations of ligand-bound PYLs, the PYLs family can be divided into three subclasses, among which the trans-dimeric subclass, represented by PYL3, reveals a distinct regulatory mechanism. PubMed: 22579247DOI: 10.1016/j.str.2012.02.019 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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