1v1f | pdb_00001v1f

Structure of the Arabidopsis thaliana SOS3 complexed with Calcium(II) and Manganese(II) ions

spinqualitylabelsall models 1v1f, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1v1f is a 1 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 3Å Ligands: CA, IOD, MN, MPD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CNBL4_ARATH Acts as a calcium sensor involved in the regulatory pathway for the control of intracellular Na(+) and K(+) homeostasis and salt tolerance. Operates in synergy with CIPK24/SOS2 to activate the plasma membrane Na(+)/H(+) antiporter SOS1. May function as positive regulator of salt stress responses. CBL proteins interact with CIPK serine-threonine protein kinases. Binding of a CBL protein to the regulatory NAF domain of a CIPK protein lead to the activation of the kinase in a calcium-dependent manner. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The Arabidopsis thaliana SOS3 gene encodes a calcium sensor that is required for plant salt tolerance. The SOS3 protein binds to and activates the self-inhibited SOS2 protein kinase, which mediates the expression and activities of various transporters important for ion homeostasis under salt stress. SOS3 belongs to a unique family of calcium-binding proteins that contain two pairs of EF hand motifs with four putative metal-binding sites. We report the crystal structure of a dimeric SOS3 protein in complex with calcium, and with calcium and manganese. Analytical ultracentrifugation experiments and circular dichroism measurements show that calcium binding is responsible for the dimerization of SOS3. This leads to a change in the global shape and surface properties of the protein that may be sufficient to transmit the Ca(2+) signal elicited during salt stress. The structure of the Arabidopsis thaliana SOS3: molecular mechanism of sensing calcium for salt stress response.,Sanchez-Barrena MJ, Martinez-Ripoll M, Zhu JK, Albert A J Mol Biol. 2005 Feb 4;345(5):1253-64. Epub 2004 Dec 8. PMID:15644219 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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