Crystallisation and preliminary X-ray diffraction analysis of FabG from Yersinia pestis.

Jeffrey Nanson, Jade Forwood

Research output: Contribution to journalArticle

4 Citations (Scopus)
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Abstract

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.
Original languageEnglish
Pages (from-to)101-104
Number of pages4
JournalActa Crystallographica Section F:Structural Biology Communications
Volume70
Issue number1
Early online date2013
DOIs
Publication statusPublished - Jan 2014

Grant Number

  • FT120100242

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