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Title: Elucidation of transient protein-protein interactions within carrier protein-dependent biosynthesis

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 inEscherichia coli. This technique describes and compares the molecular basis of six discrete binding events responsible forE. coliFAB and offers insights into a method to characterize these events and those in related carrier protein-dependent pathways.

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Publication Date:
Journal Name:
Communications Biology
Nature Publishing Group
Sponsoring Org:
National Science Foundation
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