Backbone assignment of the N-terminal 24-kDa fragment of Escherichia coli topoisomerase IV ParE subunit

Backbone assignment of the N-terminal 24-kDa fragment of Escherichia coli topoisomerase IV ParE subunit
Title:
Backbone assignment of the N-terminal 24-kDa fragment of Escherichia coli topoisomerase IV ParE subunit
Other Titles:
Biomolecular NMR Assignments
Publication Date:
19 October 2015
Citation:
Li, Y., Wong, Y.L., Lee, M.Y. et al. Biomol NMR Assign (2016) 10: 135. doi:10.1007/s12104-015-9652-9
Abstract:
Bacterial DNA topoisomerases are important drug targets due to their importance in DNA replication and low homology to human topoisomerases. The N-terminal 24kDa 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.
License type:
PublisherCopyrights
Funding Info:
A*STAR JCO grants (1331A028, 1231B015)
Description:
ISSN:
1874-2718
Files uploaded:

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