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

Title:

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

Creator:

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

Identifier:

https://cdk.lib.cas.cz/client/handle/uuid:be9e8aab-607c-4394-806e-f5d7d96051bf
uuid:be9e8aab-607c-4394-806e-f5d7d96051bf

Subject:

Lipid kinase, Calcium, Phosphatidylinositol, and Crystal structure

Type:

article, model:article, and TEXT

Description:

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.

Language:

English

Rights:

http://creativecommons.org/publicdomain/mark/1.0/
policy:public

Source:

Physiological research | 2016 Volume:65 | Number:6

Harvested from:

CDK

Metadata only:

false