Molecular basis for interactions between an acyl carrier protein and a ketosynthase.

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 ?-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.

SUBMITTER: Milligan JC 

PROVIDER: S-EPMC7323458 | biostudies-literature | 2019 Jul

REPOSITORIES: biostudies-literature