4PLA

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

4PLA の概要

• エントリーDOI: 10.2210/pdb4pla/pdb
• 分子名称: Chimera protein of Phosphatidylinositol 4-kinase type 2-alpha and Lysozyme, ADENOSINE-5'-TRIPHOSPHATE (3 entities in total)
• 機能のキーワード: phosphatidyl inositol, 4-kinase, atp, lipid, transferase, hydrolase
• 由来する生物種: Homo sapiens (Human); 詳細
• 細胞内の位置: Golgi apparatus, trans-Golgi network membrane ; Lipid- anchor : Q9BTU6
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 64255.28

構造登録者

Baumlova, A.,Chalupska, D.,Boura, E. (登録日: 2014-05-16, 公開日: 2014-09-10, 最終更新日: 2023-12-27)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.771 Å)