Characterization of the interaction between E. coli topoisomerase IV E subunit and an ATP competitive inhibitor.

Characterization of the interaction between E. coli topoisomerase IV E subunit and an ATP competitive inhibitor.
Title:
Characterization of the interaction between E. coli topoisomerase IV E subunit and an ATP competitive inhibitor.
Other Titles:
Biochemical and Biophysical Research Communications
Publication Date:
17 October 2015
Citation:
Yan Li, Ying Lei Wong, Fui Mee Ng, Boping Liu, Yun Xuan Wong, Zhi Ying Poh, Siew Wen Then, Michelle Yueqi Lee, Hui Qi Ng, Alvin W. Hung, Joseph Cherian, Jeffrey Hill, Thomas H. Keller, CongBao Kang, Characterization of the interaction between Escherichia coli topoisomerase IV E subunit and an ATP competitive inhibitor, Biochemical and Biophysical Research Communications, Volume 467, Issue 4, 27 November 2015, Pages 961-966, ISSN 0006-291X, http://dx.doi.org/10.1016/j.bbrc.2015.10.036.
Abstract:
Bacterial topoisomerase IV (ParE) is essential for DNA replication and serves as an attractive target for antibacterial drug development. The X-ray structure of the N-terminal 24 kDa ParE, responsible for ATP binding has been solved. Due to the accessibility of structural information of ParE, many potent ParE inhibitors have been discovered. In this study, a pyridylurea lead molecule against ParE of E. coli (eParE) was characterized with a series of biochemical and biophysical techniques. More importantly, solution NMR analysis of compound binding to eParE provides better understanding of the molecular interactions between the inhibitor and eParE.
License type:
http://creativecommons.org/licenses/by-nc-nd/4.0/
Funding Info:
A*STAR BMRC and JCO grants (1331A028, 1231B015)
Description:
ISSN:
0006-291X
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