PDBsum entry 3khe

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protein ligands metals Protein-protein interface(s) links
Metal binding protein PDB id
Protein chains
184 a.a. *
GOL ×3
_MG ×3
_CA ×8
Waters ×364
* Residue conservation analysis
PDB id:
Name: Metal binding protein
Title: Crystal structure of the calcium-loaded calmodulin-like doma cdpk, 541.M00134 from toxoplasma gondii
Structure: Calmodulin-like domain protein kinase isoform 3. Chain: a, b. Engineered: yes
Source: Toxoplasma gondii. Organism_taxid: 5811. Gene: tgme49_105860. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
1.95Å     R-factor:   0.204     R-free:   0.277
Authors: A.K.Wernimont,A.Hutchinson,J.D.Artz,F.Mackenzie,D.Cossar, I.Kozieradzki,C.H.Arrowsmith,A.M.Edwards,C.Bountra,J.Weigel A.Bochkarev,R.Hui,W.Qiu,M.Amani,Structural Genomics Consort
Key ref: A.K.Wernimont et al. (2011). Structures of parasitic CDPK domains point to a common mechanism of activation. Proteins, 79, 803-820. PubMed id: 21287613
30-Oct-09     Release date:   19-Jan-10    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
Q3HNM6  (Q3HNM6_TOXGO) -  Calcium-dependent protein kinase CDPK3
537 a.a.
184 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Calcium/calmodulin-dependent protein kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + a protein = ADP + a phosphoprotein
+ protein
+ phosphoprotein
      Cofactor: Ca(2+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biochemical function     calcium ion binding     1 term  


Proteins 79:803-820 (2011)
PubMed id: 21287613  
Structures of parasitic CDPK domains point to a common mechanism of activation.
A.K.Wernimont, M.Amani, W.Qiu, J.C.Pizarro, J.D.Artz, Y.H.Lin, J.Lew, A.Hutchinson, R.Hui.
We recently determined the first structures of inactivated and calcium-activated calcium-dependent protein kinases (CDPKs) from Apicomplexa. Calcium binding triggered a large conformational change that constituted a new mechanism in calcium signaling and a novel EF-hand fold (CAD, for CDPK activation domain). Thus we set out to determine if this mechanism was universal to all CDPKs. We solved additional CDPK structures, including one from the species Plasmodium. We highlight the similarities in sequence and structure across apicomplexan and plant CDPKs, and strengthen our observations that this novel mechanism could be universal to canonical CDPKs. Our new structures demonstrate more detailed steps in the mechanism of calcium activation and possible key players in regulation. Residues involved in making the largest conformational change are the most conserved across Apicomplexa, leading us to propose that the mechanism is indeed conserved. CpCDPK3_CAD and PfCDPK_CAD were captured at a possible intermediate conformation, lending insight into the order of activation steps. PfCDPK3_CAD adopts an activated fold, despite having an inactive EF-hand sequence in the N-terminal lobe. We propose that for most apicomplexan CDPKs, the mode of activation will be similar to that seen in our structures, while specific regulation of the inactive and active forms will require further investigation.