Crystal structure of fatty acid thioesterase A bound by 129 fragments provides diverse development opportunities.

ABSTRACT:

Background

In order to alleviate the growing issue of herbicide resistance, diversification of the herbicide portfolio is necessary. A promising yet underutilized mode-of-action is the inhibition of fatty acid thioesterases (FATs), which terminate de novo fatty acid (FA) biosynthesis by releasing FAs from acyl carrier protein (ACP) cofactors. These enzymes impact plant growth and sterility by determining the amount and length of FAs present. In this study we report a crystallographic fragment screening approach for the identification of novel chemical matter targeting FATs.

Results

We have solved the crystal structure of Arabidopsis thaliana FatA to 1.5 Å and conducted a crystallographic fragment screen which identified 129 unique fragments bound in 141 different poses. Ten

SUBMITTER: Kot E 

PROVIDER: S-EPMC12713704 | biostudies-literature | 2026 Jan

REPOSITORIES: biostudies-literature