Structural insights into Escherichia coli phosphopantothenoylcysteine synthetase by native ion mobility-mass spectrometry.
Accepted version
Peer-reviewed
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Repository DOI
Change log
Authors
Chan, Daniel Shiu-Hin
Hess, Jeannine https://orcid.org/0000-0001-5916-0728
Shaw, Elen
Spry, Christina
Starley, Robert
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.
Description
Keywords
Carboxy-Lyases, Dimerization, Drug Evaluation, Preclinical, Enzyme Inhibitors, Escherichia coli, Escherichia coli Proteins, Kinetics, Mass Spectrometry, Multienzyme Complexes, Peptide Synthases, Protein Domains
Journal Title
Biochem J
Conference Name
Journal ISSN
0264-6021
1470-8728
1470-8728
Volume Title
476
Publisher
Portland Press Ltd.
Publisher DOI
Rights
All rights reserved
Sponsorship
Bill & Melinda Gates Foundation (via Foundation for the National Institutes of Health (FNIH)) (BLUN17STB)
European Commission Horizon 2020 (H2020) Marie Sklodowska-Curie actions (789607)
European Commission Horizon 2020 (H2020) Marie Sklodowska-Curie actions (789607)