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

Thanh Thi Ngoc Doan, Jin Kwang Kim, Qui Khanh Mac, Cheolwon Chung, Natarajan Sampath, Jeong Gu Kim, Yeh Jin Ahn, Lin Woo Kang

Department of Advanced Technology Fusion, Konkuk University, Gwangjin-gu, Seoul, Republic of Korea.

Acta crystallographica. Section F, Structural biology and crystallization communications 2011 Dec 1

filter terms:

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 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.

Citation

Thanh Thi Ngoc Doan, Jin Kwang Kim, Qui Khanh Mac, Cheolwon Chung, Natarajan Sampath, Jeong Gu Kim, Yeh Jin Ahn, Lin Woo Kang. Crystallization and preliminary X-ray crystallographic analysis of β-ketoacyl-ACP synthase I (XoFabB) from Xanthomonas oryzae pv. oryzae. Acta crystallographica. Section F, Structural biology and crystallization communications. 2011 Dec 1;67(Pt 12):1548-50