9HRQ

Crystal structure of Arabidopsis thaliana Fatty Acid Thioesterase A with an unidentified ligand which closes the N-terminal domain

Summary for 9HRQ

• Entry DOI: 10.2210/pdb9hrq/pdb
• Descriptor: Oleoyl-acyl carrier protein thioesterase 1, chloroplastic, SULFATE ION, UNKNOWN LIGAND, ... (4 entities in total)
• Functional Keywords: thioesterase, plant, fatty acid biosynthesis, fatty acid, chain termination, dimer, hydrolase, acyl-acp thioesterase, acyl acp thioesterase, 18:1 fa, fata, acp, herbicide, mode of action
• Biological source: Arabidopsis thaliana (thale cress)
• Total number of polymer chains: 2
• Total formula weight: 67345.27

Authors

Kot, E.,Ni, X.,Koekemoer, L.,Mulholland, N.P.,Montgomery, M.G.,von Delft, F. (deposition date: 2024-12-18, release date: 2025-08-13, Last modification date: 2026-03-04)

Primary citation

Kot, E.,Ferla, M.P.,Hollinshead, P.H.,Tomlinson, C.W.E.,Fearon, D.,Aschenbrenner, J.C.,Koekemoer, L.,Winokan, M.,Fairhead, M.,Ni, X.,Chalk, R.,England, K.S.,Varga, L.O.,Montgomery, M.G.,Mulholland, N.P.,von Delft, F.
Crystal structure of fatty acid thioesterase A bound by 129 fragments provides diverse development opportunities.
Pest Manag Sci, 82:151-168, 2026

PubMed Abstract: 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.

PubMed: 40936424
DOI: 10.1002/ps.70199

Experimental method

X-RAY DIFFRACTION (1.54 Å)