Kirkpatrick Andrew S, Yokoyama Takeshi, Choi Kyoung-Jae, Yeo Hye-Jeong
Department of Biology and Biochemistry, University of Houston, 4800 Calhoun, Houston, TX 77204, USA.
Biochem Biophys Res Commun. 2009 Mar 6;380(2):407-12. doi: 10.1016/j.bbrc.2009.01.115.
Fatty acid biosynthesis is crucial for all living cells. In contrast to higher organisms, bacteria use a type II fatty acid synthase (FAS II) composed of a series of individual proteins, making FAS II enzymes excellent targets for antibiotics discovery. The beta-hydroxyacyl-ACP dehydratase (FabZ) catalyzes an essential step in the FAS II pathway. Here, we report the structure of Campylobacter jejuni FabZ (CjFabZ), showing a hexamer both in crystals and solution, with each protomer adopting the characteristic hot dog fold. Together with biochemical analysis of CjFabZ, we define the first functional FAS II enzyme from this pathogen, and provide a framework for investigation on roles of FAS II in C. jejuni virulence.
脂肪酸生物合成对所有活细胞都至关重要。与高等生物不同,细菌使用由一系列单个蛋白质组成的II型脂肪酸合酶(FAS II),这使得FAS II酶成为发现抗生素的极佳靶点。β-羟基酰基-ACP脱水酶(FabZ)催化FAS II途径中的一个关键步骤。在此,我们报道了空肠弯曲菌FabZ(CjFabZ)的结构,显示其在晶体和溶液中均为六聚体,每个原体采用典型的热狗折叠结构。结合对CjFabZ的生化分析,我们确定了来自这种病原体的首个功能性FAS II酶,并为研究FAS II在空肠弯曲菌毒力中的作用提供了一个框架。