4v29

The crystal structure of Arabidopsis thaliana CAR4 in complex with two calcium ions

spinqualitylabelsall models 4v29, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4v29 is a 2 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 1.6Å Ligands: CA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CAR4_ARATH Mediates the transient calcium-dependent interaction of PYR/PYL/RCAR abscisic acid (ABA) receptors with the plasma membrane and thus regulates ABA sensitivity (PubMed:26719420, PubMed:25465408). Stimulates the GTPase/ATPase activities of YchF1, and regulates its subcellular localization. Promotes tolerance towards salinity stress by limiting the accumulation of reactive oxygen species (ROS) (PubMed:23550829). Promotes resistance to bacterial pathogens (e.g. Xanthomonas oryzae pv. oryzae and P. syringae pv. tomato DC3000) (By similarity). Binds liposomes in the absence of exogenous Ca(2+), but this activity is enhanced in the presence of Ca(2+) and generates membrane curvature (PubMed:26719420).[UniProtKB:Q6YWF1] Publication Abstract from PubMed Membrane-delimited abscisic acid (ABA) signal transduction plays a critical role in early ABA signaling, but the molecular mechanisms linking core signaling components to the plasma membrane are unclear. We show that transient calcium-dependent interactions of PYR/PYL ABA receptors with membranes are mediated through a 10-member family of C2-domain ABA-related (CAR) proteins in Arabidopsis thaliana. Specifically, we found that PYL4 interacted in an ABA-independent manner with CAR1 in both the plasma membrane and nucleus of plant cells. CAR1 belongs to a plant-specific gene family encoding CAR1 to CAR10 proteins, and bimolecular fluorescence complementation and coimmunoprecipitation assays showed that PYL4-CAR1 as well as other PYR/PYL-CAR pairs interacted in plant cells. The crystal structure of CAR4 was solved, which revealed that, in addition to a classical calcium-dependent lipid binding C2 domain, a specific CAR signature is likely responsible for the interaction with PYR/PYL receptors and their recruitment to phospholipid vesicles. This interaction is relevant for PYR/PYL function and ABA signaling, since different car triple mutants affected in CAR1, CAR4, CAR5, and CAR9 genes showed reduced sensitivity to ABA in seedling establishment and root growth assays. In summary, we identified PYR/PYL-interacting partners that mediate a transient Ca2+-dependent interaction with phospholipid vesicles, which affects PYR/PYL subcellular localization and positively regulates ABA signaling. C2-Domain Abscisic Acid-Related Proteins Mediate the Interaction of PYR/PYL/RCAR Abscisic Acid Receptors with the Plasma Membrane and Regulate Abscisic Acid Sensitivity in Arabidopsis.,Rodriguez L, Gonzalez-Guzman M, Diaz M, Rodrigues A, Izquierdo-Garcia AC, Peirats-Llobet M, Fernandez MA, Antoni R, Fernandez D, Marquez JA, Mulet JM, Albert A, Rodriguez PL Plant Cell. 2014 Dec 2. pii: tpc.114.129973. PMID:25465408 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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