期刊
NATURE CHEMICAL BIOLOGY
卷 15, 期 7, 页码 669-+出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/s41589-019-0301-y
关键词
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资金
- 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
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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