Journal article
Bacterial structural genomics target enabled by a recently discovered potent fungal acetyl-CoA synthetase inhibitor
Acta crystallographica. Section F, Structural biology communications, Vol.79, pp.137-143
06/01/2023
DOI: 10.1107/S2053230X23003801
PMCID: PMC10231259
PMID: 37223974
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.
Details
- Title: Subtitle
- Bacterial structural genomics target enabled by a recently discovered potent fungal acetyl-CoA synthetase inhibitor
- Creators
- Nicholas D DeBouver - UCB Pharma (Belgium)Madison J Bolejack - UCB Pharma (United States)Taiwo E Esan - Northern Illinois UniversityDamian J Krysan - University of IowaTimothy J Hagen - Northern Illinois UniversityJan Abendroth - UCB Pharma (Belgium)
- Resource Type
- Journal article
- Publication Details
- Acta crystallographica. Section F, Structural biology communications, Vol.79, pp.137-143
- DOI
- 10.1107/S2053230X23003801
- PMID
- 37223974
- PMCID
- PMC10231259
- NLM abbreviation
- Acta Crystallogr F Struct Biol Commun
- eISSN
- 2053-230X
- Grant note
- HHSN272201700059C / NIAID NIH HHS
- Language
- English
- Date published
- 06/01/2023
- Academic Unit
- Molecular Physiology and Biophysics; Microbiology and Immunology; Stead Family Department of Pediatrics; Infectious Disease (Pediatrics)
- Record Identifier
- 9984419457402771
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