PDBsum entry 2ehb

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protein metals Protein-protein interface(s) links
Signalling protein/transferase PDB id
Protein chains
182 a.a. *
126 a.a. *
_CA ×2
Waters ×210
* Residue conservation analysis
PDB id:
Name: Signalling protein/transferase
Title: The structure of thE C-terminal domain of the protein kinase bound to the calcium sensor atsos3
Structure: Calcineurin b-like protein 4. Chain: a. Fragment: residues in database 1-207. Synonym: protein salt overly sensitive 3, sos3. Engineered: yes. Cbl-interacting serine/threonine-protein kinase 2 chain: d. Fragment: c-terminal domain (residues 304-446). Synonym: salt overly sensitive 2 protein, sos2, snf1-relate
Source: Arabidopsis thaliana. Thale cress. Organism_taxid: 3702. Gene: sos3. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: sos2.
2.10Å     R-factor:   0.217     R-free:   0.259
Authors: M.J.Sanchez-Barrena
Key ref:
M.J.Sánchez-Barrena et al. (2007). The Structure of the C-Terminal Domain of the Protein Kinase AtSOS2 Bound to the Calcium Sensor AtSOS3. Mol Cell, 26, 427-435. PubMed id: 17499048 DOI: 10.1016/j.molcel.2007.04.013
06-Mar-07     Release date:   25-Sep-07    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
O81223  (CNBL4_ARATH) -  Calcineurin B-like protein 4
222 a.a.
182 a.a.
Protein chain
Pfam   ArchSchema ?
Q9LDI3  (CIPKO_ARATH) -  CBL-interacting serine/threonine-protein kinase 24
446 a.a.
126 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chain D: E.C.  - Non-specific serine/threonine protein kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + a protein = ADP + a phosphoprotein
+ protein
+ phosphoprotein
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     membrane   5 terms 
  Biological process     stomatal movement   7 terms 
  Biochemical function     protein binding     4 terms  


DOI no: 10.1016/j.molcel.2007.04.013 Mol Cell 26:427-435 (2007)
PubMed id: 17499048  
The Structure of the C-Terminal Domain of the Protein Kinase AtSOS2 Bound to the Calcium Sensor AtSOS3.
M.J.Sánchez-Barrena, H.Fujii, I.Angulo, M.Martínez-Ripoll, J.K.Zhu, A.Albert.
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.
  Selected figure(s)  
Figure 2.
Figure 2. Structural Comparison of SOS3 and Related Structures
(A) Stereoview of the superimposition of the ribbon diagrams corresponding to the structures of the SOS3-FISL/NAF domain (orange/blue) and the unbound form of SOS3 (green) (PDB code 1V1G).
(B) Structure of the SOS3-FISL/FISL domain (left) and the structurally related complexes is shown: the regulatory and catalytic subunits of calcineurin (center, PDB code 1TCO) and the cacineurin B homologous protein and the plasma membrane Na/H exchanger (right, PDB code 2BEC).
Figure 5.
Figure 5. Relevant Interactions between the SOS3-FISL/NAF Domain and the PPI Domain
A section of the structure of the regulatory domain of SOS2 and SOS3 showing the residues interacting with Arg340. The labeled residues are within 3.8 Å sphere around Arg340. The straight dashed lines stand for the hydrogen bonds. Residues belonging to the SOS3-FISL/NAF domain are depicted in green. Residues belonging to the PPI domain are depicted in orange.
  The above figures are reprinted by permission from Cell Press: Mol Cell (2007, 26, 427-435) copyright 2007.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21047983 J.Rivandi, J.Miyazaki, M.Hrmova, M.Pallotta, M.Tester, and N.C.Collins (2011).
A SOS3 homologue maps to HvNax4, a barley locus controlling an environmentally sensitive Na+ exclusion trait.
  J Exp Bot, 62, 1201-1216.  
20974737 P.Coello, S.J.Hey, and N.G.Halford (2011).
The sucrose non-fermenting-1-related (SnRK) family of protein kinases: potential for manipulation to improve stress tolerance and increase yield.
  J Exp Bot, 62, 883-893.  
21145462 K.Moravcevic, J.M.Mendrola, K.R.Schmitz, Y.H.Wang, D.Slochower, P.A.Janmey, and M.A.Lemmon (2010).
Kinase associated-1 domains drive MARK/PAR1 kinases to membrane targets by binding acidic phospholipids.
  Cell, 143, 966-977.
PDB codes: 3ose 3osm 3ost
19247687 A.M.Bertorello, and J.K.Zhu (2009).
SIK1/SOS2 networks: decoding sodium signals via calcium-responsive protein kinase pathways.
  Pflugers Arch, 458, 613-619.  
  19826238 C.G.Xie, H.Lin, X.W.Deng, and Y.Guo (2009).
Roles of SCaBP8 in salt stress response.
  Plant Signal Behav, 4, 956-958.  
19054707 S.Luan (2009).
The CBL-CIPK network in plant calcium signaling.
  Trends Plant Sci, 14, 37-42.  
19860013 S.Weinl, and J.Kudla (2009).
The CBL-CIPK Ca(2+)-decoding signaling network: function and perspectives.
  New Phytol, 184, 517-528.  
18320589 C.Carrière, J.P.Mornon, C.Venien-Bryan, N.Boisset, and I.Callebaut (2008).
Calcineurin B-like domains in the large regulatory alpha/beta subunits of phosphorylase kinase.
  Proteins, 71, 1597-1606.  
  17620712 M.J.Sánchez-Barrena, S.Moreno-Pérez, I.Angulo, M.Martínez-Ripoll, and A.Albert (2007).
The complex between SOS3 and SOS2 regulatory domain from Arabidopsis thaliana: cloning, expression, purification, crystallization and preliminary X-ray analysis.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 63, 568-570.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.