PMID:11173491
| Citation |
Jia, Z, Cottrill, M, Pal, GP, Lee, D, Sung, M, Forsberg, CW and Phillips, JP (2001) Purification, crystallization and preliminary X-ray analysis of the Escherichia coli glucose-1-phosphatase. Acta Crystallogr. D Biol. Crystallogr. 57:314-6 |
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| Abstract |
Encoded by the agp gene, Escherichia coli glucose-1-phosphatase hydrolyzes glucose-1-phosphate in the periplasmic space of the bacterium. It is a potential drug-design target because inositol phosphatases have been identified as important virulence determinants in several human and animal pathogens. The enzyme was isolated and purified to homogeneity from a strain of E. coli CU1867 (an appA-deficient mutant). Crystals were obtained overnight by the equilibrium vapour-diffusion method from a solution containing 10 mg ml(-1) enzyme, 1.2 M ammonium sulfate and 25% polyethylene glycol monomethyl ether 5000 in 0.1 M MES at pH 6.5. The crystals belong to space group R3, with unit-cell parameters a = b = 156.0, c = 92.2 A. The diffraction limit was 2.6 A at a rotating-anode X-ray source; a 2.7 A resolution data set has been collected using light mineral oil as a cryoprotectant. The data set was 95.2% complete, with an R(sym) of 0.058. There were two monomers of glucose-1-phosphatase in the asymmetric unit, which correspond to a V(M) of 2.36 A Da(-1) and 47.5% solvent content. Self-rotation analysis unambiguously shows a twofold non-crystallographic symmetry. |
| Links | |
| Keywords |
Crystallization; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli Proteins; Phosphoric Monoester Hydrolases/chemistry; Phosphoric Monoester Hydrolases/genetics; Phosphoric Monoester Hydrolases/isolation & purification; Protein Conformation; X-Ray Diffraction |
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