3HZT

Crystal structure of Toxoplasma gondii CDPK3, TGME49_105860

Summary for 3HZT

• Entry DOI: 10.2210/pdb3hzt/pdb
• Related: 3HX4
• Descriptor: Calcium-dependent protein kinase 3, MAGNESIUM ION, GLYCEROL, ... (5 entities in total)
• Functional Keywords: calcium dependent kinase, calmodulin, troponin parasite, structural genomics, structural genomics consortium, sgc, atp-binding, kinase, nucleotide-binding, serine/threonine-protein kinase, transferase
• Biological source: Toxoplasma gondii
• Total number of polymer chains: 1
• Total formula weight: 54602.91

Authors

Wernimont, A.K.,Artz, J.D.,Finnerty, P.,Wasney, G.,Allali-Hassani, A.,Vedadi, M.,Bochkarev, A.,Arrowsmith, C.H.,Edwards, A.M.,Bountra, C.,Weigelt, J.,Hui, R.,Amani, M.,Structural Genomics Consortium (SGC) (deposition date: 2009-06-24, release date: 2009-07-21, Last modification date: 2023-09-06)

Primary citation

Wernimont, A.K.,Artz, J.D.,Finerty, P.,Lin, Y.H.,Amani, M.,Allali-Hassani, A.,Senisterra, G.,Vedadi, M.,Tempel, W.,Mackenzie, F.,Chau, I.,Lourido, S.,Sibley, L.D.,Hui, R.
Structures of apicomplexan calcium-dependent protein kinases reveal mechanism of activation by calcium.
Nat.Struct.Mol.Biol., 17:596-601, 2010

PubMed Abstract: Calcium-dependent protein kinases (CDPKs) have pivotal roles in the calcium-signaling pathway in plants, ciliates and apicomplexan parasites and comprise a calmodulin-dependent kinase (CaMK)-like kinase domain regulated by a calcium-binding domain in the C terminus. To understand this intramolecular mechanism of activation, we solved the structures of the autoinhibited (apo) and activated (calcium-bound) conformations of CDPKs from the apicomplexan parasites Toxoplasma gondii and Cryptosporidium parvum. In the apo form, the C-terminal CDPK activation domain (CAD) resembles a calmodulin protein with an unexpected long helix in the N terminus that inhibits the kinase domain in the same manner as CaMKII. Calcium binding triggers the reorganization of the CAD into a highly intricate fold, leading to its relocation around the base of the kinase domain to a site remote from the substrate binding site. This large conformational change constitutes a distinct mechanism in calcium signal-transduction pathways.

PubMed: 20436473
DOI: 10.1038/nsmb.1795

Experimental method

X-RAY DIFFRACTION (2 Å)