Figure 3
From: Coenzyme A binding sites induce proximal acylation across protein families
Structural modeling of CoA conformation reveals proximal hyperacylation near CoA-binding sites (a) Schematic diagram of the computational approach used to calculate the minimal distance between a lysine residue the CoA’s thiol group in a protein CoA-binding pocket. A conformational ensemble of physically plausible CoA conformation was made by combining experimentally observed bond rotational angles from CoA crystal structures after the phospho-ADP moiety. Full structural models of CoA-binding proteins from acylomic datasets were generated using Swissmodel. The CoA ensemble was docked into each protein model to generate a set of sterically accessible CoA thiol locations and used to score each modeled lysine residue’s amine-thiol distance. (b) Table showing the numbers of non-acylated and acylated lysine residues found on CoA-binding proteins. Relative odds ratio for CoA-reachable lysines (< 5 Å from the nearest CoA ensemble sulfur) being acylated vs. more distal lysine residues were calculated for each of acetylation, succinylation, and glutarylation. The significance of the results was calculated using Fisher’s exact test. (c) Relative probability of lysine acylation on CoA binding protein lysines as a function of a lysine’s distance from the CoA ensemble. Data shown for acetylation, succinylation, and glutarylation.
