Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4TZ7

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

Summary for 4TZ7
Entry DOI10.2210/pdb4tz7/pdb
DescriptorPhosphatidylinositol-4-phosphate 5-kinase, type I, alpha (1 entity in total)
Functional Keywordskinase, transferase
Biological sourceDanio rerio (Zebrafish)
Total number of polymer chains1
Total formula weight44869.31
Authors
Hu, J.,Qin, Y.,Wang, J.,Li, L.,Wu, D.,Ha, Y. (deposition date: 2014-07-09, release date: 2015-09-02, Last modification date: 2023-12-27)
Primary citationHu, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.31 Å)
Structure validation

238582

PDB entries from 2025-07-09

PDB statisticsPDBj update infoContact PDBjnumon