| Literature DB >> 31488574 |
Daniel Shiu-Hin Chan1, Jeannine Hess1, Elen Shaw1, Christina Spry1, Robert Starley1, Claudio Dagostin1, Marcio V B Dias2, Ramesh Kale1, Vitor Mendes2, Tom L Blundell2, Anthony G Coyne1, Chris Abell1.
Abstract
CoaBC, part of the vital coenzyme A biosynthetic pathway in bacteria, has recently been validated as a promising antimicrobial target. In this work, we employed native ion mobility-mass spectrometry to gain structural insights into the phosphopantothenoylcysteine synthetase domain of E. coli CoaBC. Moreover, native mass spectrometry was validated as a screening tool to identify novel inhibitors of this enzyme, highlighting the utility and versatility of this technique both for structural biology and for drug discovery.Entities:
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Year: 2019 PMID: 31488574 DOI: 10.1042/BCJ20190318
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857