1. Molecular basis for interactions between an acyl carrier protein and a ketosynthase
- Author
-
Michael D. Burkart, Joseph J. Hale, Shiou-Chuan Tsai, D. John Lee, David R. Jackson, Ray Luo, Jesus F. Barajas, Joris Beld, Andrew J. Schaub, and Jacob C. Milligan
- Subjects
Models, Molecular ,Biochemistry & Molecular Biology ,Fatty Acid Synthases ,1.1 Normal biological development and functioning ,Fatty acid synthase complex ,Crystallography, X-Ray ,medicine.disease_cause ,Type II ,Article ,Medicinal and Biomolecular Chemistry ,03 medical and health sciences ,chemistry.chemical_compound ,Biosynthesis ,Models ,Underpinning research ,3-Oxoacyl-(Acyl-Carrier-Protein) Synthase ,Fatty Acid Synthase, Type II ,Escherichia coli ,Acyl Carrier Protein ,medicine ,2.1 Biological and endogenous factors ,Transferase ,Aetiology ,Molecular Biology ,030304 developmental biology ,chemistry.chemical_classification ,0303 health sciences ,Crystallography ,biology ,Chemistry ,Escherichia coli Proteins ,030302 biochemistry & molecular biology ,Molecular ,Fatty acid ,Cell Biology ,Nuclear magnetic resonance spectroscopy ,Acyl carrier protein ,Biochemistry ,Fatty Acid Synthase ,X-Ray ,biology.protein ,lipids (amino acids, peptides, and proteins) ,Biochemistry and Cell Biology ,Protein Binding - 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. A combination of crosslinking, X-ray crystallography, NMR, and mutagenesis provide a detailed visualization of the interactions between an acyl carrier protein and β-ketoacyl-ACP-synthase I in the Escherchia coli fatty acid synthase complex.
- Published
- 2019