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PDBsum entry 3k21
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* Residue conservation analysis
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PDB id:
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Transferase
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Title:
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Crystal structure of carboxy-terminus of pfc0420w.
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Structure:
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Calcium-dependent protein kinase 3. Chain: a. Synonym: pfcdpk3. Engineered: yes
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Source:
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Plasmodium falciparum. Organism_taxid: 5833. Gene: cdpk3, cpk3, mal3p3.17, pfc0420w. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
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Resolution:
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1.15Å
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R-factor:
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0.152
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R-free:
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0.186
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Authors:
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A.K.Wernimont,A.Hutchinson,J.D.Artz,F.Mackenzie,D.Cossar, I.Kozieradzki,C.H.Arrowsmith,A.M.Edwards,C.Bountra,J.Weigelt, A.Bochkarev,R.Hui,M.Amani,Structural Genomics Consortium (Sgc)
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Key ref:
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A.K.Wernimont
et al.
(2011).
Structures of parasitic CDPK domains point to a common mechanism of activation.
Proteins,
79,
803-820.
PubMed id:
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Date:
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29-Sep-09
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Release date:
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26-Jan-10
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PROCHECK
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Headers
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References
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Q9NJU9
(CDPK3_PLAF7) -
Calcium-dependent protein kinase 3 from Plasmodium falciparum (isolate 3D7)
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Seq:
Struc:
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562 a.a.
178 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 5 residue positions (black
crosses)
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Enzyme class:
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E.C.2.7.11.1
- non-specific serine/threonine protein kinase.
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Reaction:
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1.
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L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H+
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2.
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L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H+
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L-seryl-[protein]
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+
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ATP
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=
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O-phospho-L-seryl-[protein]
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+
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ADP
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+
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H(+)
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L-threonyl-[protein]
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+
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ATP
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=
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O-phospho-L-threonyl-[protein]
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+
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ADP
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+
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H(+)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Proteins
79:803-820
(2011)
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PubMed id:
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Structures of parasitic CDPK domains point to a common mechanism of activation.
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A.K.Wernimont,
M.Amani,
W.Qiu,
J.C.Pizarro,
J.D.Artz,
Y.H.Lin,
J.Lew,
A.Hutchinson,
R.Hui.
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ABSTRACT
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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.
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Links
