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Molecular basis for interactions between an acyl carrier protein and a ketosynthase
- Milligan, Jacob C;
- Lee, D John;
- Jackson, David R;
- Schaub, Andrew J;
- Beld, Joris;
- Barajas, Jesus F;
- Hale, Joseph J;
- Luo, Ray;
- Burkart, Michael D;
- Tsai, Shiou-Chuan
Published Web Location
https://doi.org/10.1038/s41589-019-0301-yAbstract
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.
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