NDLI: Structures of apicomplexan calcium-dependent protein kinases reveal mechanism of activation by calcium

Content Provider	PubMed Central
Author	Wernimont, Amy K. Artz, Jennifer D. Finerty, Patrick Lin, Y. Amani, Mehrnaz Abdellah, Allali-hassani Guillermo, Senisterra Masoud, Vedadi Tempel, Wolfram Mackenzie, Farrell Chau, Irene Lourido, Sebastian Sibley, L. David Hui, Raymond
Abstract	Calcium-dependent protein kinases (CDPKs) play pivotal roles in the calcium-signaling pathway in plants, ciliates and apicomplexan parasites, and comprise a 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.
Related Links	http://dx.doi.org/10.1038/nsmb.1795
Ending Page	601
Page Count	6
Starting Page	596
File Format	PDF
ISSN	15459993
e-ISSN	15459985
Journal	Nature structural & molecular biology
Issue Number	5
Volume Number	17
Language	English
Publisher Date	2010-05-01
Access Restriction	Open
Subject Keyword	Molecular Biology Structural Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Structural Biology Molecular Biology

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