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Molecular basis for interactions between an acyl carrier protein and a ketosynthase
Journal article   Open access   Peer reviewed

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

Jacob C. Milligan, D. John Lee, David R. Jackson, Andrew J. Schaub, Joris Beld, Jesus F. Barajas, Joseph J. Hale, Ray Luo, Michael D. Burkart and Shiou-Chuan Tsai
Nature chemical biology, v 15(7), pp 669-671
01 Jul 2019
PMID: 31209348
url
https://europepmc.org/articles/pmc7323458View
Accepted (AM)Open Access (License Unspecified) Open

Abstract

Biochemistry & Molecular Biology Life Sciences & Biomedicine Science & Technology
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 beta-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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Biochemistry & Molecular Biology
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