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The structural basis for calcium inhibition of lipid kinase PI4K IIalpha and comparison with the apo state

A. Baumlova, J. Gregor, E. Boura,

. 2016 ; 65 (6) : 987-993. [pub] 20160819

Language English Country Czech Republic

Document type Journal Article

Persistent link   https://www.medvik.cz/link/bmc17012793

PI4K IIalpha is a critical enzyme for the maintenance of Golgi and is also known to function in the synaptic vesicles. The product of its catalytical function, phosphatidylinositol 4-phosphate (PI4P), is an important lipid molecule because it is a hallmark of the Golgi and TGN, is directly recognized by many proteins and also serves as a precursor molecule for synthesis of higher phosphoinositides. Here, we report crystal structures of PI4K IIalpha enzyme in the apo-state and inhibited by calcium. The apo-structure reveals a surprising rigidity of the active site residues important for catalytic activity. The structure of calcium inhibited kinase reveals how calcium locks ATP in the active site.

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