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PDBsum entry 3k21

Go to PDB code: 
protein ligands metals links
Transferase PDB id
3k21
Jmol
Contents
Protein chain
178 a.a. *
Ligands
PEG ×2
GOL
ACT
Metals
_CA ×3
Waters ×233
* Residue conservation analysis
PDB id:
3k21
Name: Transferase
Title: Crystal structure of carboxy-terminus of pfc0420w.
Structure: Calcium-dependent protein kinase 3. Chain: a. Synonym: pfcdpk3. Engineered: yes
Source: Plasmodium falciparum. Organism_taxid: 5833. Gene: cdpk3, cpk3, mal3p3.17, pfc0420w. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
Resolution:
1.15Å     R-factor:   0.152     R-free:   0.186
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,M.Amani,Structural Genomics Consortium (S
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
Date:
29-Sep-09     Release date:   26-Jan-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q9NJU9  (CDPK3_PLAF7) -  Calcium-dependent protein kinase 3
Seq:
Struc:
 
Seq:
Struc:
562 a.a.
178 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 5 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.2.7.11.1  - Non-specific serine/threonine protein kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + a protein = ADP + a phosphoprotein
ATP
+ protein
= ADP
+ phosphoprotein
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  

 

 
    reference    
 
 
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.
 
  ABSTRACT  
 
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.