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Updated: Jan 23, 2026

Detection of Protein S-Acylation using Acyl-Resin Assisted Capture
Published on: April 10, 2020
Molecular basis for interactions between an acyl carrier protein and a ketosynthase
Jacob C Milligan1, D John Lee2, David R Jackson3
1Department of Molecular Biology and Biochemistry, University of California, Irvine, Irvine, CA, USA.
Abstract:
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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