Premium
Crystallization and preliminary X‐ray diffraction analysis of FabG from Yersinia pestis
Author(s) -
Nanson Jeffrey David,
Forwood Jade Kenneth
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x13033402
Subject(s) - yersinia pestis , crystallization , bacteria , biosynthesis , stereochemistry , reductase , fatty acid synthesis , chemistry , biology , virulence , crystallography , fatty acid , biochemistry , enzyme , gene , organic chemistry , genetics
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 ( yp FabG), 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 P 2 1 2 1 2 1 symmetry, with unit‐cell parameters a = 68.22, b = 98.68, c = 169.84 Å, and four yp FabG molecules in the asymmetric unit.