Protein-protein interaction based substrate control in the E. coli octanoic acid transferase, LipB.

ABSTRACT: Lipoic acid is an essential cofactor produced in all organisms by diverting octanoic acid derived as an intermediate of type II fatty acid biosynthesis. In bacteria, octanoic acid is transferred from the acyl carrier protein (ACP) to the lipoylated target protein by the octanoyltransferase LipB. LipB has a well-documented substrate selectivity, indicating a mechanism of octanoic acid recognition. The present study reveals the precise protein-protein interactions (PPIs) responsible for this selectivity in Escherichia coli through a combination of solution-state protein NMR titration with high-resolution docking of the experimentally examined substrates. We examine the structural changes of substrate-bound ACP and determine the precise geometry of the LipB interface. Thermodynamic eff

SUBMITTER: Bartholow TG 

PROVIDER: S-EPMC8495967 | biostudies-literature | 2021 Oct

REPOSITORIES: biostudies-literature