5JO1

Crystal structure of phaseic acid-bound abscisic acid receptor PYL3 in complex with type 2C protein phosphatase HAB1

Summary for 5JO1

• Entry DOI: 10.2210/pdb5jo1/pdb
• Related: 5JNN 5JO2
• Descriptor: Protein phosphatase 2C 16, Abscisic acid receptor PYL3, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: aba receptor, phaseic acid, hab1, pyr/pyl, signaling protein-hydrolase complex, signaling protein/hydrolase
• Biological source: Arabidopsis thaliana (Mouse-ear cress); More
• Total number of polymer chains: 2
• Total formula weight: 58348.26

Authors

Weng, J.K.,Noel, J.P. (deposition date: 2016-05-01, release date: 2016-09-07, Last modification date: 2024-03-06)

Primary citation

Weng, J.K.,Ye, M.,Li, B.,Noel, J.P.
Co-evolution of Hormone Metabolism and Signaling Networks Expands Plant Adaptive Plasticity.
Cell, 166:881-893, 2016

PubMed Abstract: Classically, hormones elicit specific cellular responses by activating dedicated receptors. Nevertheless, the biosynthesis and turnover of many of these hormone molecules also produce chemically related metabolites. These molecules may also possess hormonal activities; therefore, one or more may contribute to the adaptive plasticity of signaling outcomes in host organisms. Here, we show that a catabolite of the plant hormone abscisic acid (ABA), namely phaseic acid (PA), likely emerged in seed plants as a signaling molecule that fine-tunes plant physiology, environmental adaptation, and development. This trait was facilitated by both the emergence-selection of a PA reductase that modulates PA concentrations and by the functional diversification of the ABA receptor family to perceive and respond to PA. Our results suggest that PA serves as a hormone in seed plants through activation of a subset of ABA receptors. This study demonstrates that the co-evolution of hormone metabolism and signaling networks can expand organismal resilience.

PubMed: 27518563
DOI: 10.1016/j.cell.2016.06.027

Experimental method

X-RAY DIFFRACTION (2.3 Å)