4tz7 | pdb_00004tz7

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

spinqualitylabelsall models 4tz7, resolution 3.31Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4tz7 is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Publication Abstract from PubMed 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 A 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. Resolution of structure of PIP5K1A reveals molecular mechanism for its regulation by dimerization and dishevelled.,Hu J, Yuan Q, Kang X, Qin Y, Li L, Ha Y, Wu D Nat Commun. 2015 Sep 14;6:8205. doi: 10.1038/ncomms9205. PMID:26365782 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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