Department of Molecular Biology and Biochemistry, University of California, Irvine, Irvine, CA, USA.
Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA, USA.
Nat Chem Biol. 2019 Jul;15(7):669-671. doi: 10.1038/s41589-019-0301-y. Epub 2019 Jun 17.
Fatty acid synthases are dynamic ensembles of enzymes that can biosynthesize long hydrocarbon chains efficiently. Here we visualize the interaction between the Escherichia coli acyl carrier protein (AcpP) and β-ketoacyl-ACP-synthase I (FabB) using X-ray crystallography, NMR, and molecular dynamics simulations. We leveraged this structural information to alter lipid profiles in vivo and provide a molecular basis for how protein-protein interactions can regulate the fatty acid profile in E. coli.
脂肪酸合酶是一种动态的酶复合物，能够有效地生物合成长链烃。在这里，我们使用 X 射线晶体学、NMR 和分子动力学模拟技术可视化了大肠杆菌酰基辅酶 A 载体蛋白（AcpP）和β-酮酰-ACP 合酶 I（FabB）之间的相互作用。我们利用这些结构信息在体内改变脂质谱，并为蛋白质-蛋白质相互作用如何调节大肠杆菌中的脂肪酸谱提供了分子基础。
