BioDesign 2023; 11(3): 50-54
Published online September 30, 2023
© Korean Society for Structural Biology
Shanru He1,2 and Yongbin Xu1,2,*
1Department of Bioengineering, College of Life Science, Dalian Minzu University, Dalian 116600, Liaoning, China
2Key Laboratory of Biotechnology and Bioresources Utilization of Ministry of Education, College of Life Science, Dalian Minzu University, Dalian 116600, Liaoning, China
Correspondence to: *firstname.lastname@example.org
3-ketoacyl-acyl carrier protein (ACP) reductase is a vital enzyme in the biosynthesis of fatty acids in bacteria and plants. It assumes a critical role in the elongation process of fatty acids. The enzyme’s primary function is to catalyze the reduction of a 3-ketoacyl-ACP intermediate, forming a fully saturated acyl-ACP. This saturated acyl-ACP can subsequently elongate within the fatty acid synthesis pathway. This study successfully expressed and purified FnFabG from Fusobacterium nucleatum using Ni-NTA affinity and gel-filtration chromatography. The protein crystal was obtained and diffracted to a resolution of 2.7 Å. The preliminary crystallographic analysis suggested that FnFabG crystal belongs to the monoclinic space group P41212 with a = b = 111.56 Å and c = 88.69 Å, α = β = γ = 90.00°. The asymmetric unit contained one molecule of FnFabG, giving a solvent content of 78.33%.