TY - JOUR
T1 - Crystallization and preliminary X-ray diffraction analysis of FabG from Yersinia pestis
AU - Nanson, Jeffrey
AU - Forwood, Jade
N1 - Includes bibliographical references.
PY - 2014/1
Y1 - 2014/1
N2 - 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. [beta]-Ketoacyl-ACP reductase (FabG) is responsible for the reduction of the [beta]-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 P212121 symmetry, with unit-cell parameters a = 68.22, b = 98.68, c = 169.84 Å, and four ypFabG molecules in the asymmetric unit.
AB - 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. [beta]-Ketoacyl-ACP reductase (FabG) is responsible for the reduction of the [beta]-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 P212121 symmetry, with unit-cell parameters a = 68.22, b = 98.68, c = 169.84 Å, and four ypFabG molecules in the asymmetric unit.
KW - ketoacyl-ACP reductase
KW - FabG
KW - Yersina pestis
UR - http://www.scopus.com/inward/record.url?scp=84905400416&partnerID=8YFLogxK
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U2 - 10.1107/S2053230X13033402
DO - 10.1107/S2053230X13033402
M3 - Article
C2 - 24419628
SN - 1744-3091
VL - 70
SP - 101
EP - 104
JO - Acta Crystallographica Section F:Structural Biology Communications
JF - Acta Crystallographica Section F:Structural Biology Communications
IS - 1
ER -