Literature summary for 2.7.1.127 extracted from

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

Search for more literature for 2.7.1.127

Cloned(Commentary)

Cloned (Comment)	Organism
expression of mutant cDNA fragment encoding for residues 185-459 of the catalytic domain of isozyme A as unlabeled or selenomethionine-labeled GST fusion proteins in Escherichia coli	Rattus norvegicus

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant unlabeled or selennomethionine-labeled mutant catalytic domain residues 185-459, 10 mg/ml protein in 25 mM Tris-HCl, pH 8.0, 150 mM NaCl, and 10 mM DTT, crystallization solution contains 2.2 M ammonium sulfate, 0.2 M sodium formate, 10 mM DTT, 10 mM ADP, 10 mM 1D-myo-inositol 1,3,4,5-tetrakisphosphate, and 10 mM MgCl2, cryoprotection of crystals by successive transfer into 5-15% glycerol in mother liquor, X-ray diffraction structure determination and analysis at 2.2 A resolution	Rattus norvegicus

Crystallization (Comment)

Organism

purified recombinant unlabeled or selennomethionine-labeled mutant catalytic domain residues 185-459, 10 mg/ml protein in 25 mM Tris-HCl, pH 8.0, 150 mM NaCl, and 10 mM DTT, crystallization solution contains 2.2 M ammonium sulfate, 0.2 M sodium formate, 10 mM DTT, 10 mM ADP, 10 mM 1D-myo-inositol 1,3,4,5-tetrakisphosphate, and 10 mM MgCl2, cryoprotection of crystals by successive transfer into 5-15% glycerol in mother liquor, X-ray diffraction structure determination and analysis at 2.2 A resolution

Rattus norvegicus

Protein Variants

Protein Variants	Comment	Organism
D423N	crystal structure determination and analysis	Rattus norvegicus
L217M	crystal structure determination and analysis	Rattus norvegicus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	-	Rattus norvegicus

Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	-	isozyme A	-

Purification (Commentary)

Purification (Comment)	Organism
unlabeled or selenomethionine-labeled recombinant residues 185-459 of the catalytic domain of isozyme A fused to GST from Escherichia coli by glutathione affinity chromatography, removal of the GST-tag by recombinant TEV protease, further purification by a second step of glutathione affinity chromatography, adsorption chromatography, and gel filtration	Rattus norvegicus

Reaction

Reaction	Comment	Organism	Reaction ID
ATP + 1D-myo-inositol 1,4,5-trisphosphate = ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate	catalytic core structure, substrate binding and catalytic mechanism, structure-function realtionship	Rattus norvegicus	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + 1D-myo-inositol 1,4,5-trisphosphate	-	Rattus norvegicus	ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate	-	?
additional information	the enzyme contains a catalytic domain and a 4-helix substrate binding domain, both are in an open conformation with respect to each other, thus substrate recognition and catalysis involve a dynamic conformational cycle	Rattus norvegicus	?	-	?

Subunits

Subunits	Comment	Organism
More	the enzyme contains a catalytic domain and a 4-helix substrate binding domain, both are in an open conformation with respect to each other, thus substrate recognition and catalysis involve a dynamic conformational cycle	Rattus norvegicus

Synonyms

Synonyms	Comment	Organism
inositol 1,4,5-trisphosphate 3-kinase	-	Rattus norvegicus
IP3KA	-	Rattus norvegicus
More	the enzyme is a member of the protein kinase superfamily	Rattus norvegicus

Cofactor

Cofactor	Comment	Organism	Structure
ATP	binding site structure	Rattus norvegicus