2EHB

The structure of the C-terminal domain of the protein kinase AtSOS2 bound to the calcium sensor AtSOS3

Summary for 2EHB

• Entry DOI: 10.2210/pdb2ehb/pdb
• Descriptor: Calcineurin B-like protein 4, CBL-interacting serine/threonine-protein kinase 24, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: protein complex, ca(ii) ions bound to sos3 (ef-hands 1 and 4), sos2 fisl motif, sos2 phosphatase binding domain (ppi), signalling protein-transferase complex, signalling protein/transferase
• Biological source: Arabidopsis thaliana (thale cress); More
• Cellular location: Cell membrane; Lipid-anchor: O81223
• Total number of polymer chains: 2
• Total formula weight: 40494.89

Authors

Sanchez-Barrena, M.J. (deposition date: 2007-03-06, release date: 2007-09-25, Last modification date: 2024-04-03)

Primary citation

Sanchez-Barrena, M.J.,Fujii, H.,Angulo, I.,Martinez-Ripoll, M.,Zhu, J.K.,Albert, A.
The structure of the C-terminal domain of the protein kinase AtSOS2 bound to the calcium sensor AtSOS3
Mol.Cell, 26:427-435, 2007

PubMed Abstract: The plant SOS2 family of protein kinases and their interacting activators, the SOS3 family of calcium-binding proteins, function together in decoding calcium signals elicited by different environmental stimuli. SOS2 is activated by Ca-SOS3 and subsequently phosphorylates the ion transporter SOS1 to bring about cellular ion homeostasis under salt stress. In addition to possessing the kinase activity, members of the SOS2 family of protein kinases can bind to protein phosphatase 2Cs. The crystal structure of the binary complex of Ca-SOS3 with the C-terminal regulatory moiety of SOS2 resolves central questions regarding the dual function of SOS2 as a kinase and a phosphatase-binding protein. A comparison with the structure of unbound SOS3 reveals the basis of the molecular function of this family of kinases and their interacting calcium sensors. Furthermore, our study suggests that the structure of the phosphatase-interaction domain of SOS2 defines a scaffold module conserved from yeast to human.

PubMed: 17499048
DOI: 10.1016/j.molcel.2007.04.013

Experimental method

X-RAY DIFFRACTION (2.1 Å)