Bacterial Structural Genomics Target Enabled by Recently Discovered Potent Fungal ACS Inhibitor
Nicholas D. DeBouver, Madison J. Bolejack, Taiwo E. Esan, Damian J. Krysan, Timothy J. Hagen, Jan Abendroth [1]
Molecular Tour
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 for a previously elusive structural genomics target. of L. pneumophila ACS. Orange indicates the N-terminal domain, maroon is the C-terminal domain, dark green is the NT-Ext domain, cyan is the hinge region, lime green is the ATP-binding loop, yellow is bound ethyl-AMP. (7mmz). . 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.
References
- ↑ doi: https://dx.doi.org/10.1107/S2053230X23003801
