7MMZ
Crystal Structure of Acetyl-coenzyme A synthetase from Legionella pneumophila Philadelphia 1 in complex with ethyl-AMP
Summary for 7MMZ
| Entry DOI | 10.2210/pdb7mmz/pdb |
| Descriptor | Acetyl-coenzyme A synthetase, 5'-O-[(S)-ethoxy(hydroxy)phosphoryl]adenosine, 1,2-ETHANEDIOL, ... (4 entities in total) |
| Functional Keywords | ssgcid, acetyl-coenzyme a synthetase, acs-1, legionella pneumophila, structural genomics, seattle structural genomics center for infectious disease, ligase |
| Biological source | Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513) |
| Total number of polymer chains | 1 |
| Total formula weight | 71068.82 |
| Authors | Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2021-04-30, release date: 2021-05-26, Last modification date: 2023-10-25) |
| Primary citation | DeBouver, N.D.,Bolejack, M.J.,Esan, T.E.,Krysan, D.J.,Hagen, T.J.,Abendroth, J. Bacterial structural genomics target enabled by a recently discovered potent fungal acetyl-CoA synthetase inhibitor. Acta Crystallogr.,Sect.F, 2023 Cited by PubMed 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. PubMed: 37223974DOI: 10.1107/S2053230X23003801 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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