Journal:Acta Cryst F:S2053230X23003801

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<b>Molecular Tour</b><br>
<b>Molecular Tour</b><br>
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. 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.
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. 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.
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<scene name='96/963801/Structure/1'>Structure</scene> of ''L. pneumophila'' ACS. Red indicates the CTD, Orange is the NTD, Dark green is the NT-Ext domain, cyan is the hinge region, lime green is the ATP-binding loop, yellow is bound ethyl-AMP.
<b>References</b><br>
<b>References</b><br>

Revision as of 14:29, 3 May 2023

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