학술논문
The structural basis for calcium inhibition of lipid kinase PI4K IIα and comparison with the apo state.
Document Type
TEXT
Author
Source
Physiological research | 2016 Volume:65 | Number:6
Subject
Language
English
Abstract
PI4K IIα 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 IIα 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.