1V1G
Structure of the Arabidopsis thaliana SOS3 complexed with Calcium(II) ion
Summary for 1V1G
| Entry DOI | 10.2210/pdb1v1g/pdb |
| Related | 1V1F |
| Descriptor | CALCINEURIN B-LIKE PROTEIN 4, IODIDE ION, CALCIUM ION, ... (5 entities in total) |
| Functional Keywords | signalling protein, salt stress response in plants, calcineurin b-like protein, protein crystallography, calcium sensor, ef-hand |
| Biological source | ARABIDOPSIS THALIANA (MOUSE-EAR CRESS) |
| Total number of polymer chains | 1 |
| Total formula weight | 27013.48 |
| Authors | Sanchez-Barrena, M.J.,Martinez-Ripoll, M.,Zhu, J.K.,Albert, A. (deposition date: 2004-04-15, release date: 2005-01-19, Last modification date: 2024-05-08) |
| Primary citation | Sanchez-Barrena, M.J.,Martinez-Ripoll, M.,Zhu, J.K.,Albert, A. The Structure of the Arabidopsis Thaliana SOS3: Molecular Mechanism of Sensing Calcium for Salt Stress Response J.Mol.Biol., 345:1253-, 2005 Cited by PubMed Abstract: 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. PubMed: 15644219DOI: 10.1016/J.JMB.2004.11.025 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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