3HX4
Crystal structure of CDPK1 of Toxoplasma gondii, TGME49_101440, in presence of calcium
Summary for 3HX4
| Entry DOI | 10.2210/pdb3hx4/pdb |
| Descriptor | Calmodulin-domain protein kinase 1, CALCIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (6 entities in total) |
| Functional Keywords | cdpks, toxoplasma, kinase, protist, structural genomics, structural genomics consortium, sgc, atp-binding, nucleotide-binding, serine/threonine-protein kinase, transferase |
| Biological source | Toxoplasma gondii |
| Total number of polymer chains | 1 |
| Total formula weight | 58721.10 |
| Authors | Wernimont, A.K.,Artz, J.D.,Finnerty, P.,Xiao, T.,He, H.,MacKenzie, F.,Sinestera, G.,Hassani, A.A.,Wasney, G.,Vedadi, M.,Lourido, S.,Bochkarev, A.,Arrowsmith, C.H.,Edwards, A.M.,Bountra, C.,Weigelt, J.,Sibley, D.L.,Hui, R.,Lin, Y.H.,Structural Genomics Consortium (SGC) (deposition date: 2009-06-19, release date: 2009-07-21, Last modification date: 2024-02-21) |
| 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 Cited by 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: 20436473DOI: 10.1038/nsmb.1795 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
Download full validation report
