4n0g

Crystal Structure of PYL13-PP2CA complex

spinqualitylabelsall models 4n0g, resolution 2.38Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4n0g is a 4 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.382Å Ligands: MG, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function P2C37_ARATH Major negative regulator of abscisic acid (ABA) responses during seed germination and cold acclimation. Confers insensitivity to ABA. Modulates negatively the AKT2/3 activity, which mediates K(+) transport and membrane polarization during stress situations, probably by dephosphorylation. Prevent stomata closure by inactivating the S-type anion efflux channel SLAC1 and its activator SRK2E. Publication Abstract from PubMed PYR1/PYL/RCAR family proteins (PYLs) are well-characterized abscisic acid (ABA) receptors. Among the 14 PYL members in Arabidopsis thaliana, PYL13 is ABA irresponsive and its function has remained elusive. Here, we show that PYL13 selectively inhibits the phosphatase activity of PP2CA independent of ABA. The crystal structure of PYL13-PP2CA complex, which was determined at 2.4 A resolution, elucidates the molecular basis for the specific recognition between PP2CA and PYL13. In addition to the canonical interactions between PYLs and PP2Cs, an extra interface is identified involving an element in the vicinity of a previously uncharacterized CCCH zinc-finger (ZF) motif in PP2CA. Sequence blast identified another 56 ZF-containing PP2Cs, all of which are from plants. The structure also reveals the molecular determinants for the ABA irresponsiveness of PYL13. Finally, biochemical analysis suggests that PYL13 may hetero-oligomerize with PYL10. These two PYLs antagonize each other in their respective ABA-independent inhibitions of PP2Cs. The biochemical and structural studies provide important insights into the function of PYL13 in the stress response of plant and set up a foundation for future biotechnological applications of PYL13.Cell Research advance online publication 29 October 2013; doi:10.1038/cr.2013.143. Molecular basis for the selective and ABA-independent inhibition of PP2CA by PYL13.,Li W, Wang L, Sheng X, Yan C, Zhou R, Hang J, Yin P, Yan N Cell Res. 2013 Oct 29. doi: 10.1038/cr.2013.143. PMID:24165892 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Abscisic acid receptor 3D structures Protein phosphatase 3D structures

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