Crystallization and preliminary X-ray crystallographic analysis of β-ketoacyl-ACP synthase I (XoFabB) from Xanthomonas oryzae pv. oryzae.

ABSTRACT: The proteins in the fatty-acid synthesis pathway in bacteria have significant potential as targets for the development of antibacterial agents. An essential elongation step in fatty-acid synthesis is performed by β-ketoacyl-acyl carrier protein synthase I (FabB). The organism Xanthomonas oryzae pv. oryzae (Xoo) causes a destructive bacterial blight disease of rice. The XoFabB protein from Xoo was expressed, purified and crystallized for the three-dimensional structure determination that is essential for the development of specific inhibitors of the enzyme. An XoFabB crystal diffracted to 3.0 Å resolution and belonged to the tetragonal space group P4(1), with unit-cell parameters a = b = 82.2, c = 233.2 Å. Assuming that the crystallographic structure contains four molecules in the asymmetri

SUBMITTER: Doan TT 

PROVIDER: S-EPMC3232136 | biostudies-literature | 2011 Dec

REPOSITORIES: biostudies-literature