3UJL

Crystal structure of abscisic acid bound PYL2 in complex with type 2C protein phosphatase ABI2

Summary for 3UJL

• Entry DOI: 10.2210/pdb3ujl/pdb
• Related: 3UJG 3UJK
• Descriptor: Abscisic acid receptor PYL2, Protein phosphatase 2C 77, (2Z,4E)-5-[(1S)-1-hydroxy-2,6,6-trimethyl-4-oxocyclohex-2-en-1-yl]-3-methylpenta-2,4-dienoic acid, ... (5 entities in total)
• Functional Keywords: pyl2, abscisic receptor, abi2, protein phosphatase 2c, aba signaling, signaling protein
• Biological source: Arabidopsis thaliana (mouse-ear cress,thale-cress); More
• Cellular location: Cytoplasm (By similarity): O80992
• Total number of polymer chains: 2
• Total formula weight: 56026.63

Authors

Zhou, X.E.,Soon, F.-F.,Ng, L.-M.,Kovach, A.,Tan, M.H.E.,Suino-Powell, K.M.,He, Y.,Xu, Y.,Brunzelle, J.S.,Li, J.,Melcher, K.,Xu, H.E. (deposition date: 2011-11-07, release date: 2012-02-15, Last modification date: 2024-10-09)

Primary citation

Soon, F.F.,Ng, L.M.,Zhou, X.E.,West, G.M.,Kovach, A.,Tan, M.H.,Suino-Powell, K.M.,He, Y.,Xu, Y.,Chalmers, M.J.,Brunzelle, J.S.,Zhang, H.,Yang, H.,Jiang, H.,Li, J.,Yong, E.L.,Cutler, S.,Zhu, J.K.,Griffin, P.R.,Melcher, K.,Xu, H.E.
Molecular mimicry regulates ABA signaling by SnRK2 kinases and PP2C phosphatases.
Science, 335:85-88, 2012

PubMed Abstract: Abscisic acid (ABA) is an essential hormone for plants to survive environmental stresses. At the center of the ABA signaling network is a subfamily of type 2C protein phosphatases (PP2Cs), which form exclusive interactions with ABA receptors and subfamily 2 Snfl-related kinase (SnRK2s). Here, we report a SnRK2-PP2C complex structure, which reveals marked similarity in PP2C recognition by SnRK2 and ABA receptors. In the complex, the kinase activation loop docks into the active site of PP2C, while the conserved ABA-sensing tryptophan of PP2C inserts into the kinase catalytic cleft, thus mimicking receptor-PP2C interactions. These structural results provide a simple mechanism that directly couples ABA binding to SnRK2 kinase activation and highlight a new paradigm of kinase-phosphatase regulation through mutual packing of their catalytic sites.

PubMed: 22116026
DOI: 10.1126/science.1215106

Experimental method

X-RAY DIFFRACTION (2.5 Å)