Abstract
Fatty acid biosynthesis (FAB) is an essential and highly conserved metabolic pathway. In bacteria, this process is mediated by an elaborate network of protein•protein interactions (PPIs) involving a small, dynamic acyl carrier protein that interacts with dozens of other partner proteins (PPs). These PPIs have remained poorly characterized due to their dynamic and transient nature. Using a combination of solution-phase NMR spectroscopy and protein-protein docking simulations, we report a comprehensive residue-by-residue comparison of the PPIs formed during FAB in Escherichia coli. This technique describes and compares the molecular basis of six discrete binding events responsible for E. coli FAB and offers insights into a method to characterize these events and those in related carrier protein-dependent pathways.
Publication types
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Comparative Study
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Research Support, N.I.H., Extramural
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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 / metabolism
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Acetyltransferases / metabolism
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Acyl Carrier Protein / metabolism*
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Alcohol Oxidoreductases / metabolism
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Binding Sites
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Enoyl-(Acyl-Carrier-Protein) Reductase (NADH) / metabolism
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Escherichia coli / enzymology*
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Escherichia coli Proteins / metabolism*
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Fatty Acid Synthase, Type II / metabolism*
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Fatty Acids / biosynthesis*
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Lysophospholipase / metabolism
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Molecular Docking Simulation
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Periplasmic Proteins / metabolism
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Protein Binding
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Protein Interaction Domains and Motifs
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Proton Magnetic Resonance Spectroscopy
Substances
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Acyl Carrier Protein
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Escherichia coli Proteins
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Fatty Acids
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Periplasmic Proteins
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acpP protein, E coli
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Alcohol Oxidoreductases
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acetoacetyl-CoA reductase
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Enoyl-(Acyl-Carrier-Protein) Reductase (NADH)
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fabI protein, E coli
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Acetyltransferases
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fabF protein, E coli
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3-Oxoacyl-(Acyl-Carrier-Protein) Synthase
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FabB protein, E coli
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Lysophospholipase
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tesA protein, E coli
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Fatty Acid Synthase, Type II