PMID:10944349
| Citation |
Garrido Franco, M, Huber, R, Schmidt, FS, Laber, B and Clausen, T (2000) Crystallization and preliminary X-ray crystallographic analysis of PdxJ, the pyridoxine 5'-phosphate synthesizing enzyme. Acta Crystallogr. D Biol. Crystallogr. 56:1045-8 |
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| Abstract |
The enzyme PdxJ catalyzes the condensation of 1-deoxy-D-xylulose-5-phosphate (DXP) and 1-amino-3-oxo-4-(phosphohydroxy)propan-2-one to form pyridoxine 5'-phosphate (PNP). The protein from Escherichia coli has been crystallized in several forms under different conditions. The best diffracting crystals were obtained by a combination of the hanging-drop vapour-diffusion and microseeding techniques. Using an in-house image plate, the PdxJ crystals diffracted under cryo-conditions to 2.6 A resolution. The space group has been determined as C222(1), with unit-cell parameters a = 132.5, b = 154. 4, c = 131.4 A, corresponding to four monomers per asymmetric unit. In the search for heavy-atom derivatives, a mercury derivative has been interpreted. The 12 mercury sites located are related by 222 symmetry and, in combination with self-rotation search analyses and gel-filtration experiments, indicate the quaternary assembly of PdxJ into octamers with 422 symmetry. |
| Links | |
| Keywords |
Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Crystallization; Crystallography, X-Ray; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli Proteins; Ligases; Protein Structure, Quaternary; Pyridoxal Phosphate/analogs & derivatives; Pyridoxal Phosphate/biosynthesis |
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