1TZD

CRYSTAL STRUCTURE OF THE CATALYTIC CORE OF INOSITOL 1,4,5-TRISPHOSPHATE 3-KINASE

Summary for 1TZD

• Entry DOI: 10.2210/pdb1tzd/pdb
• Descriptor: Inositol-trisphosphate 3-kinase A, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: inositol kinase, transferase
• Biological source: Rattus norvegicus (Norway rat)
• Total number of polymer chains: 2
• Total formula weight: 64460.90

Authors

Miller, G.J.,Hurley, J.H. (deposition date: 2004-07-09, release date: 2004-09-21, Last modification date: 2024-11-20)

Primary citation

Miller, G.J.,Hurley, J.H.
Crystal structure of the catalytic core of inositol 1,4,5-trisphosphate 3-kinase
Mol.Cell, 15:703-711, 2004

PubMed Abstract: Soluble inositol polyphosphates are ubiquitous second messengers in eukaryotes, and their levels are regulated by an array of specialized kinases. The structure of an archetypal member of this class, inositol 1,4,5-trisphosphate 3-kinase (IP3K), has been determined at 2.2 angstroms resolution in complex with magnesium and adenosine diphosphate. IP3K contains a catalytic domain that is a variant of the protein kinase superfamily, and a novel four-helix substrate binding domain. The two domains are in an open conformation with respect to each other, suggesting that substrate recognition and catalysis by IP3K involves a dynamic conformational cycle. The unique helical domain of IP3K blocks access to the active site by membrane-bound phosphoinositides, explaining the structural basis for soluble inositol polyphosphate specificity.

PubMed: 15350215
DOI: 10.1016/j.molcel.2004.08.005

Experimental method

X-RAY DIFFRACTION (2.2 Å)