Bacterial structural genomics target enabled by a recently discovered potent fungal acetyl-CoA synthetase inhibitor

Acta Crystallogr F Struct Biol Commun. 2023 Jun 1;79(Pt 6):137-143. doi: 10.1107/S2053230X23003801. Epub 2023 May 24.

Abstract

The compound ethyl-adenosyl monophosphate ester (ethyl-AMP) has been shown to effectively inhibit acetyl-CoA synthetase (ACS) enzymes and to facilitate the crystallization of fungal ACS enzymes in various contexts. In this study, the addition of ethyl-AMP to a bacterial ACS from Legionella pneumophila resulted in the determination of a co-crystal structure of this previously elusive structural genomics target. The dual functionality of ethyl-AMP in both inhibiting ACS enzymes and promoting crystallization establishes its significance as a valuable resource for advancing structural investigations of this class of proteins.

Keywords: Legionella pneumophila; SSGCID; acetyl-coenzyme A synthetase; ligases; structural genomics.

MeSH terms

  • Acetyl Coenzyme A / metabolism
  • Adenosine Monophosphate / metabolism
  • Crystallography, X-Ray
  • Genomics*

Substances

  • Acetyl Coenzyme A
  • Adenosine Monophosphate