Abstract
Bacterial DNA topoisomerases are important drug targets due to their importance in DNA replication and low homology to human topoisomerases. The N-terminal 24 kDa region of E. coli topoisomerase IV E subunit (eParE) contains the ATP binding pocket. Structure—based drug discovery has been proven to be an efficient way to develop potent ATP competitive inhibitors against ParEs. NMR spectroscopy is a powerful tool to understand protein and inhibitor interactions in solution. In this study, we report the backbone assignment for the N-terminal domain of E. coli ParE. The secondary structural information and the assignment will aid in structure—based antibacterial agents development targeting eParE.
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Acknowledgments
We appreciate financial support from A*STAR JCO grants (1331A028, 1231B015). We also thank Prof Ho Sup Yoon and Dr. Hong Ye from Nanyang Technological University for the NMR experiments.
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Li, Y., Wong, Y.L., Lee, M.Y. et al. Backbone assignment of the N-terminal 24-kDa fragment of Escherichia coli topoisomerase IV ParE subunit. Biomol NMR Assign 10, 135–138 (2016). https://doi.org/10.1007/s12104-015-9652-9
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DOI: https://doi.org/10.1007/s12104-015-9652-9