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 Cited by 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: 22116026DOI: 10.1126/science.1215106 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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