Journal
NATURE CHEMICAL BIOLOGY
Volume 15, Issue 7, Pages 669-+Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/s41589-019-0301-y
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Funding
- NIH [GM093040, GM079383, GM100305, GM095970]
- National Science Foundation (NSF) Division of Integrative Organismal Systems (IOS) [1516156]
- Department of Energy (DOE) Office of Science User Facility [DE-AC02-05CH11231]
- institutional Chemical and Structural Biology Training Grant (National Institute of General Medical Sciences) [T32GM108561]
- National Science Foundation Graduate Research Fellowship
- Direct For Biological Sciences
- Division Of Integrative Organismal Systems [1516156] Funding Source: National Science Foundation
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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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