4TZ7

Crystal structure of type I phosphatidylinositol 4-phosphate 5-kinase alpha from Zebrafish

4TZ7 の概要

• エントリーDOI: 10.2210/pdb4tz7/pdb
• 分子名称: Phosphatidylinositol-4-phosphate 5-kinase, type I, alpha (1 entity in total)
• 機能のキーワード: kinase, transferase
• 由来する生物種: Danio rerio (Zebrafish)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 44869.31

構造登録者

Hu, J.,Qin, Y.,Wang, J.,Li, L.,Wu, D.,Ha, Y. (登録日: 2014-07-09, 公開日: 2015-09-02, 最終更新日: 2023-12-27)

主引用文献

Hu, J.,Yuan, Q.,Kang, X.,Qin, Y.,Li, L.,Ha, Y.,Wu, D.
Resolution of structure of PIP5K1A reveals molecular mechanism for its regulation by dimerization and dishevelled.
Nat Commun, 6:8205-8205, 2015

PubMed Abstract: Type I phosphatidylinositol phosphate kinase (PIP5K1) phosphorylates the head group of phosphatidylinositol 4-phosphate (PtdIns4P) to generate PtdIns4,5P2, which plays important roles in a wide range of cellular functions including Wnt signalling. However, the lack of its structural information has hindered the understanding of its regulation. Here we report the crystal structure of the catalytic domain of zebrafish PIP5K1A at 3.3 Å resolution. This molecule forms a side-to-side dimer. Mutagenesis study of PIP5K1A reveals two adjacent interfaces for the dimerization and interaction with the DIX domain of the Wnt signalling molecule dishevelled. Although these interfaces are located distally to the catalytic/substrate-binding site, binding to these interfaces either through dimerization or the interaction with DIX stimulates PIP5K1 catalytic activity. DIX binding additionally enhances PIP5K1 substrate binding. Thus, this study elucidates regulatory mechanisms for this lipid kinase and provides a paradigm for the understanding of PIP5K1 regulation by their interacting molecules.

PubMed: 26365782
DOI: 10.1038/ncomms9205

実験手法

X-RAY DIFFRACTION (3.31 Å)