Molecular basis for interactions between an acyl carrier protein and a ketosynthase
NATURE CHEMICAL BIOLOGY(2019)
摘要
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 .
更多查看译文
关键词
Biosynthesis,Enzymes,NMR spectroscopy,X-ray crystallography,Chemistry/Food Science,general,Biochemical Engineering,Biochemistry,Cell Biology,Bioorganic Chemistry
AI 理解论文
溯源树
样例
![](https://originalfileserver.aminer.cn/sys/aminer/pubs/mrt_preview.jpeg)
生成溯源树,研究论文发展脉络
Chat Paper
正在生成论文摘要