Structures of apicomplexan calcium-dependent protein kinases reveal mechanism of activation by calcium
作者： Amy K Wernimont , Jennifer D Artz , Patrick Finerty , Yu-Hui Lin , Mehrnaz Amani
DOI: 10.1038/NSMB.1795
关键词:
摘要: Calcium-dependent protein kinases (CDPKs) have pivotal roles in the calcium-signaling pathway plants, ciliates and apicomplexan parasites comprise a calmodulin-dependent kinase (CaMK)-like domain regulated by calcium-binding C terminus. To understand this intramolecular mechanism of activation, we solved structures autoinhibited (apo) activated (calcium-bound) conformations CDPKs from Toxoplasma gondii Cryptosporidium parvum. In apo form, C-terminal CDPK activation (CAD) resembles calmodulin with an unexpected long helix N terminus that inhibits same manner as CaMKII. Calcium binding triggers reorganization CAD into highly intricate fold, leading to its relocation around base site remote substrate site. This large conformational change constitutes distinct calcium signal-transduction pathways.
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