Journal:Acta Cryst F:S2053230X23003801
From Proteopedia
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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. | ||
| - | <scene name='96/963801/Structure/1'>Structure</scene> of ''L. pneumophila'' ACS. | + | <scene name='96/963801/Structure/1'>Structure</scene> of ''L. pneumophila'' ACS. Maroon 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. (Jezewski ''et al'', 2021<ref name='Jezewski'>PMID: 34369755</ref>) |
<b>References</b><br> | <b>References</b><br> | ||
Revision as of 11:33, 4 May 2023
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