Structural studies of MIP synthase.
The conversion of glucose 6-phosphate to 1-L-myo-inositol 1--phosphate (MIP) by 1-L-myo-inositol 1-phosphate synthase (MIP synthase) is the first committed and rate-limiting step in the de novo biosynthesis of inositol in all eukaryotes. The importance of inositol-containing molecules both as membrane components and as critical second messenger signal-transduction species make the function and regulation of this enzyme important for a host of biologically important cellular functions including proliferation, neurostimulation, secretion and contraction. MIP synthase has been overexpressed in Esherichia coli and purified to homogeneity by chromatographic methods. Two crystal forms of MIP synthase were obtained by the hanging-drop vapor-diffusion method. Native data sets for both crystal forms were collected in-house on a Rigaku R-AXIS IIC imaging-plate detector. Crystal form I belongs to space group C2, with unit-cell parameters a = 153.0, b = 96.6, c = 122.6 A, beta = 126.4 degrees, and diffracts to 2.5 A resolution. Crystal form II belongs to space group P2(1), with unit-cell parameters a = 94.5, b = 186.2, c = 86.5 A, beta = 110.5 degrees, and diffracts to 2.9 A resolution.
Stein
A J
AJ
Michigan State University, Department of Chemistry, East Lansing, MI 48824, USA.
Geiger
J H
JH
D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli; D005656:Fungal Proteins / Q000737:chemistry* / Q000302:isolation & purification; D008958:Models, Molecular; D007296:Myo-Inositol-1-Phosphate Synthase / Q000737:chemistry* / Q000302:isolation & purification; D011487:Protein Conformation; D011993:Recombinant Fusion Proteins / Q000737:chemistry; D012441:Saccharomyces cerevisiae / Q000201:enzymology*
D005656:Fungal Proteins; D011993:Recombinant Fusion Proteins; D007296:Myo-Inositol-1-Phosphate Synthase