3ZUT
The structure of OST1 (D160A) kinase
Summary for 3ZUT
| Entry DOI | 10.2210/pdb3zut/pdb |
| Related | 3ZUU |
| Descriptor | Serine/threonine-protein kinase SRK2E (2 entities in total) |
| Functional Keywords | transferase, kinase regulation, plant abiotic stress, signaling |
| Biological source | Arabidopsis thaliana (Mouse-ear cress) |
| Total number of polymer chains | 2 |
| Total formula weight | 82104.98 |
| Authors | Yunta, C.,Martinez-Ripoll, M.,Albert, A. (deposition date: 2011-07-20, release date: 2011-10-12, Last modification date: 2023-12-20) |
| Primary citation | Yunta, C.,Martinez-Ripoll, M.,Zhu, J.K.,Albert, A. The structure of Arabidopsis thaliana OST1 provides insights into the kinase regulation mechanism in response to osmotic stress. J. Mol. Biol., 414:135-144, 2011 Cited by PubMed Abstract: SnRK [SNF1 (sucrose non-fermenting-1)-related protein kinase] 2.6 [open stomata 1 (OST1)] is well characterized at molecular and physiological levels to control stomata closure in response to water-deficit stress. OST1 is a member of a family of 10 protein kinases from Arabidopsis thaliana (SnRK2) that integrates abscisic acid (ABA)-dependent and ABA-independent signals to coordinate the cell response to osmotic stress. A subgroup of protein phosphatases type 2C binds OST1 and keeps the kinase dephosphorylated and inactive. Activation of OST1 relies on the ABA-dependent inhibition of the protein phosphatases type 2C and the subsequent self-phosphorylation of the kinase. The OST1 ABA-independent activation depends on a short sequence motif that is conserved among all the members of the SnRK2 family. However, little is known about the molecular mechanism underlying this regulation. The crystallographic structure of OST1 shows that ABA-independent regulation motif stabilizes the conformation of the kinase catalytically essential α C helix, and it provides the basis of the ABA-independent regulation mechanism for the SnRK2 family of protein kinases. PubMed: 21983340DOI: 10.1016/j.jmb.2011.09.041 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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