4rj9

Structure of a plant specific C2 domain protein, OsGAP1 from rice

spinqualitylabelsall models 4rj9, resolution 1.63Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4rj9 is a 1 chain structure with sequence from Oryza sativa Japonica Group. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.63Å Ligands: K Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GAP1_ORYSJ Mediates the transient calcium-dependent interaction of PYR/PYL/RCAR abscisic acid (ABA) receptors with the plasma membrane and thus regulates ABA sensitivity (By similarity). 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:19086295, PubMed:23550829). Promotes resistance to bacterial pathogens (e.g. Xanthomonas oryzae pv. oryzae and P. syringae pv. tomato DC3000) (PubMed:19086295).[UniProtKB:Q9LVH4] Publication Abstract from PubMed The C2 domain is one of the most diverse phospholipid-binding domains mediating cellular signaling. One group of C2-domain proteins are plant-specific and are characterized by their small sizes and simple structures. We have previously reported that a member of this group, OsGAP1, is able to alleviate salt stress and stimulate defense responses, and bind to both phospholipids and an unconventional G-protein, OsYchF1. Here we solved the crystal structure of OsGAP1 to a resolution of 1.63 A. Using site-directed mutagenesis, we successfully differentiated between the clusters of surface residues that are required for binding to phospholipids versus OsYchF1, which, in turn, is critical for its role in stimulating defense responses. On the other hand, the ability to alleviate salt stress by OsGAP1 is dependent only on its ability to bind OsYchF1 and is independent of its phospholipid-binding activity. Site-Directed Mutagenesis Shows the Significance of Interactions with Phospholipids and the G-protein OsYchF1 on the Physiological Functions of the Rice GTPase-Activating Protein 1 (OsGAP1).,Yung YL, Cheung MY, Miao R, Fong YH, Li KP, Yu MH, Chye ML, Wong KB, Lam HM J Biol Chem. 2015 Aug 18. pii: jbc.M115.655639. PMID:26286751 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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