Journal:Acta Cryst F:S2053230X23003801

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. <scene name='96/963801/Structure/4'>Overall structure</scene> of ''L. pneumophila'' ACS. <span class="bg-orange">Orange indicates the N-terminal domain</span>, <span style="background-color:#800000;color:white;font-weight:bold;padding-left:0.3em;padding-right:0.3em;">maroon is the C-terminal domain</span>, <span class="bg-green text-white">dark green is the NT-Ext domain</span>, <span class="bg-cyan text-white">cyan is the hinge region</span>, <span class="bg-lightgreen">lime green is the ATP-binding loop</span>, <span class="bg-yellow">yellow is bound ethyl-AMP</span>. <scene name='96/963801/Ethyl-amp/3'>Ethyl-AMP bound to L. pneumophila ACS</scene> ([[7mmz]]). <scene name='96/963801/Sidechain_interactions/5'>Sidechain interactions between L. pneumophila ACS and ethyl-AMP</scene>, the colors as in the first scene. 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.