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.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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3-Oxoacyl-(Acyl-Carrier-Protein) Synthase / chemistry
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3-Oxoacyl-(Acyl-Carrier-Protein) Synthase / metabolism*
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Acyl Carrier Protein / chemistry
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Acyl Carrier Protein / metabolism*
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Crystallography, X-Ray
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Escherichia coli / chemistry
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Escherichia coli / enzymology
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Escherichia coli Proteins / chemistry
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Escherichia coli Proteins / metabolism*
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Fatty Acid Synthase, Type II / chemistry
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Fatty Acid Synthase, Type II / metabolism*
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Models, Molecular
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Protein Binding
Substances
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Acyl Carrier Protein
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Escherichia coli Proteins
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3-Oxoacyl-(Acyl-Carrier-Protein) Synthase
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FabB protein, E coli
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Fatty Acid Synthase, Type II