Wernimont, A.K., Artz, J.D., Finnerty, P., Lin, L., Amani, M., Schapira, M., Allali-Hassanali, A., Vedadi, M., Tempel, W., MacKenzie, F., Hui, R.
(deposited on 24.Jun.09)
Datapack version: 1 (built on 02.Dec.09; last revised in 02.Dec.09)
Calcium controls various essential pathways in apicomplexan parasites including protein secretion, motility, host invasion and egress. To mediate calcium pathways, these organisms employ calcium-dependent protein kinases (CDPK), which are also found in plants and ciliates but not in animals or fungi.
- the parasite responsible for transmission of toxoplasmosis - has a number of CDPKs in its genome, with both TgCDPK1 and TgCDPK3 characterized in previous studies[1,2].
Canonical CDPKs are comprised of a kinase domain (KD) that is highly homologous to calmodulin-dependent kinases (CaMK), followed by 4 EF-hands, which bind Ca
and play the role of intramolecular regulation. We call this regulatory domain the CDPK activation domain (CAD).
We have previously solved the structure of the KD of TgCDPK3 (3DXN). Here, we present the
(in gray) with the
intact. This structure represents the general autoinhibited form of a canonical CDPK, with the CAD resembling the
closed form of calmodulin
(3CLN) but with an
additional long helix
in the N-terminus. This helix, which we have dubbed CH1, starts a few residues downstream of the
conserved HXW motif
(X is proline in TgCDPK3) in the C-terminal lobe of the KD and spans the
and culminates in the E-helix of the
(TIP 1: the background colour can be changed to
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Kieschnick H, Wakefield T, Narducci CA, Beckers C (2001) Toxoplasma gondii attachment to host cells is regulated by a calmodulin-like domain protein kinase. J Biol Chem 276: 12369-12377.
Nagamune K, Sibley LD (2006) Comparative genomic and phylogenetic analyses of calcium ATPases and calcium-regulated proteins in the apicomplexa. Mol Biol Evol 23: 1613-1627.
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