4PLA

Crystal structure of phosphatidyl inositol 4-kinase II alpha in complex with ATP

Summary for 4PLA

• Entry DOI: 10.2210/pdb4pla/pdb
• Descriptor: Chimera protein of Phosphatidylinositol 4-kinase type 2-alpha and Lysozyme, ADENOSINE-5'-TRIPHOSPHATE (3 entities in total)
• Functional Keywords: phosphatidyl inositol, 4-kinase, atp, lipid, transferase, hydrolase
• Biological source: Homo sapiens (Human); More
• Cellular location: Golgi apparatus, trans-Golgi network membrane ; Lipid- anchor : Q9BTU6
• Total number of polymer chains: 1
• Total formula weight: 64255.28

Authors

Baumlova, A.,Chalupska, D.,Boura, E. (deposition date: 2014-05-16, release date: 2014-09-10, Last modification date: 2023-12-27)

Primary citation

Baumlova, A.,Chalupska, D.,Rozycki, B.,Jovic, M.,Wisniewski, E.,Klima, M.,Dubankova, A.,Kloer, D.P.,Nencka, R.,Balla, T.,Boura, E.
The crystal structure of the phosphatidylinositol 4-kinase II alpha.
Embo Rep., 15:1085-1092, 2014

PubMed Abstract: Phosphoinositides are a class of phospholipids generated by the action of phosphoinositide kinases with key regulatory functions in eukaryotic cells. Here, we present the atomic structure of phosphatidylinositol 4-kinase type IIα (PI4K IIα), in complex with ATP solved by X-ray crystallography at 2.8 Å resolution. The structure revealed a non-typical kinase fold that could be divided into N- and C-lobes with the ATP binding groove located in between. Surprisingly, a second ATP was found in a lateral hydrophobic pocket of the C-lobe. Molecular simulations and mutagenesis analysis revealed the membrane binding mode and the putative function of the hydrophobic pocket. Taken together, our results suggest a mechanism of PI4K IIα recruitment, regulation, and function at the membrane.

PubMed: 25168678
DOI: 10.15252/embr.201438841

Experimental method

X-RAY DIFFRACTION (2.771 Å)