3OJI

X-ray crystal structure of the Py13 -pyrabactin complex

Summary for 3OJI

• Entry DOI: 10.2210/pdb3oji/pdb
• Related: 3KL1 3KLX
• Descriptor: Abscisic acid receptor PYL3, 4-bromo-N-(pyridin-2-ylmethyl)naphthalene-1-sulfonamide, SULFATE ION, ... (4 entities in total)
• Functional Keywords: abscisic acid receptor, crystal, pp2c, pyl3, pyrabactin, hormone receptor
• Biological source: Arabidopsis thaliana (thale-cress)
• Cellular location: Cytoplasm (By similarity): Q9SSM7
• Total number of polymer chains: 2
• Total formula weight: 43585.21

Authors

Zhang, X.,Zhang, Q.,Wang, G.,Chen, Z. (deposition date: 2010-08-23, release date: 2011-08-10, Last modification date: 2023-11-01)

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

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: 22579247
DOI: 10.1016/j.str.2012.02.019

Experimental method

X-RAY DIFFRACTION (1.84 Å)