| Literature DB >> 31209348 |
Jacob C Milligan1, D John Lee2, David R Jackson3, Andrew J Schaub3, Joris Beld2, Jesus F Barajas1, Joseph J Hale2, Ray Luo1, Michael D Burkart4, Shiou-Chuan Tsai5,6,7.
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.Entities:
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Year: 2019 PMID： 31209348 PMCID： PMC7323458 DOI： 10.1038/s41589-019-0301-y
Source DB: PubMed Journal: Nat Chem Biol ISSN： 1552-4450 Impact factor: 15.040