1z2p
From Proteopedia
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Inositol 1,3,4-trisphosphate 5/6-Kinase in complex with Mg2+/AMP-PCP/Ins(1,3,4)P3
Overview
Inositol hexakisphosphate and other inositol high polyphosphates have, diverse and critical roles in eukaryotic regulatory pathways. Inositol, 1,3,4-trisphosphate 5/6-kinase catalyzes the rate-limiting step in, inositol high polyphosphate synthesis in animals. This multifunctional, enzyme also has inositol 3,4,5,6-tetrakisphosphate 1-kinase and other, activities. The structure of an archetypal family member, from Entamoeba, histolytica, has been determined to 1.2 A resolution in binary and ternary, complexes with nucleotide, substrate, and product. The structure reveals, an ATP-grasp fold. The inositol ring faces ATP edge-on such that the 5-, and 6-hydroxyl groups are nearly equidistant from the ATP gamma-phosphate, in catalytically productive phosphoacceptor positions and explains the, unusual dual site specificity of this kinase. Inositol tris- and, tetrakisphosphates interact via three phosphate binding subsites and one, solvent-exposed site that could in principle be occupied by 18 different, substrates, explaining the mechanisms for the multiple specificities and, catalytic activities of this enzyme.
About this Structure
1Z2P is a Single protein structure of sequence from Eukaryota with MG, ACP and I3S as ligands. Full crystallographic information is available from OCA.
Reference
Specificity determinants in inositol polyphosphate synthesis: crystal structure of inositol 1,3,4-trisphosphate 5/6-kinase., Miller GJ, Wilson MP, Majerus PW, Hurley JH, Mol Cell. 2005 Apr 15;18(2):201-12. PMID:15837423
Page seeded by OCA on Wed Nov 21 07:12:44 2007
Categories: Eukaryota | Single protein | Hurley, J.H. | Majerus, P.W. | Miller, G.J. | Wilson, M.P. | ACP | I3S | MG | Atp-grasp | Inositol phosphate kinase
