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2.7.1.151: inositol-polyphosphate multikinase

This is an abbreviated version!
For detailed information about inositol-polyphosphate multikinase, go to the full flat file.

Word Map on EC 2.7.1.151

Reaction

ATP
+
1D-myo-inositol 1,4,5,6-tetrakisphosphate
=
ADP
 +
1D-myo-inositol 1,3,4,5,6-pentakisphosphate

Synonyms

1,3,4,6-tetrakisphosphate 5-kinase, 5-kinase, Arg82, ArgRIII, ARGSIII, AtIpk2a, AtIpk2b, AtIpk2beta, HsIPMK, Impk, inositol 1,4,5-trisphosphate 3-kinase, inositol phosphate multikinase, inositol phosphate multikinase 2, inositol polyphosphate 6-/3-kinase, inositol polyphosphate kinase, inositol polyphosphate multikinase, Ins(1,4,5)P3 3-kinase, InsP4 5-kinase, IP3 3-kinase, IP3/IP4 6-/3-kinase, IP3K, IPK, Ipk2, Ipk2/Impk/IP3K, Ipk2a, Ipk2beta/IP3K, IPKII, IPMK, ITPK1, Kcs1, Kcs1p, More, phosphoinositol kinase, PI3K, StIPMK

ECTree

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.1 Phosphotransferases with an alcohol group as acceptor
                2.7.1.151 inositol-polyphosphate multikinase

Crystallization

Crystallization on EC 2.7.1.151 - inositol-polyphosphate multikinase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
isoform inositol phosphate multikinase alpha, to 2.9 A resolution. The structural core of Arabidopsis thaliana IPMK is homologous to those of Saccharamyces cerevisiae IPMK and Homo sapiens IP3K
purified recombinant core catalytic domain of HsIMPK, that contains residues 50 to 416, from which an internal domain comprising residues 263 to 377 is deleted and replaced with a simple Gly-Gly-Ser-Gly-Gly linker, apostructure and catalytic core domain with bound ADP-Ins (1,4,5)P3-Mg and ADP-DiC4-PtdInsP2-Mg, hanging drop vapor diffusion, mixing of 0.002 ml of 38 mg/ml protein solution with 0.002 ml of well solution containing 35% w/v PEG 400, 0.1 M Li2SO4, 100 mM MES-imidazole, pH 6.0, and 50 mM 2-mercaptoethanol, 25°C, to obtain complex structures, apoenzyme crystals are further soaked for 1 day in 35% w/v PEG 400, 100 mM Li2SO4, 100 mM HEPES, pH 7.5, at 25°C, in the presence of 20 mM Ins(1,4,5)P3 or a soluble diC4-analogue of PtdIns(4,5)P2, 10 mM MgCl2, and 5 mM of either Na2ATP or Li2AMP-PNP, X-ray diffraction structure determination and analysis at 1.63-1.93 A resolution. The structure of the IPMK apoenzyme is determined by a molecular replacement approach using a model constructed from the template of yeast ScIPMK (PDB ID 2IF8)
sitting drop vapor diffusion method. Crystal structure of the yeast inositol phosphate multikinase Ipk2 in the apoform and in a complex with ADP and Mn2+ at up to 2.0 A resolution
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Structure database comparisons of the recently solved crystal strucures of Ins(1,4,5)P3-kinase and IPMK confirm the close structural relationship to the lipid inositol kinases despite little primary amino acid sequence similarities.
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