Crystallization and preliminary X-ray diffraction analysis of FabG from Yersinia pestis.
The type II fatty-acid biosynthesis pathway of bacteria provides enormous potential for antibacterial drug development owing to the structural differences between this and the type I fatty-acid biosynthesis system found in mammals. β-Ketoacyl-ACP reductase (FabG) is responsible for the reduction of the β-ketoacyl group linked to acyl carrier protein (ACP), and is essential for the formation of fatty acids and bacterial survival. Here, the cloning, expression, purification, crystallization and diffraction of FabG from Yersinia pestis (ypFabG), the highly virulent causative agent of plague, are reported. Recombinant FabG was expressed, purified to homogeneity and crystallized via the hanging-drop vapour-diffusion technique. Diffraction data were collected at the Australian Synchrotron to 2.30 Å resolution. The crystal displayed P2(1)2(1)2(1) symmetry, with unit-cell parameters a = 68.22, b = 98.68, c = 169.84 Å, and four ypFabG molecules in the asymmetric unit.
['Nanson|Jeffrey David|JD|', 'Forwood|Jade Kenneth|JK|']
D001426:Bacterial Proteins D002846:Chromatography, Affinity D002850:Chromatography, Gel D003460:Crystallization D004591:Electrophoresis, Polyacrylamide Gel D011994:Recombinant Proteins D014961:X-Ray Diffraction D015010:Yersinia pestis
FabG β-ketoacyl-ACP reductase Yersina pestis