Open AccessCrystallization and preliminary X‐ray crystallographic analysis of β‐ketoacyl‐ACP synthase I (XoFabB) from Xanthomonas oryzae pv. oryzae
Author(s) -
Doan Thanh Thi Ngoc,
Kim JinKwang,
Mac QuiKhanh,
Chung Cheolwon,
Sampath Natarajan,
Kim JeongGu,
Ahn YehJin,
Kang LinWoo
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111040590
Subject(s) - xanthomonas oryzae , xanthomonas oryzae pv. oryzae , tetragonal crystal system , crystallization , strain (injury) , atp synthase , crystallography , xanthomonas , monomer , stereochemistry , fatty acid , enzyme , bacteria , fatty acid synthesis , biology , chemistry , crystal structure , biochemistry , organic chemistry , gene , genetics , anatomy , polymer
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 P 4 1 , with unit‐cell parameters a = b = 82.2, c = 233.2 Å. Assuming that the crystallographic structure contains four molecules in the asymmetric unit, the corresponding V M would be 2.18 Å 3 Da −1 and the solvent content would be 43.5%. The initial structure was determined by the MOLREP program with an R factor of 44.0% and does contain four monomers in the asymmetric unit.