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

Biomol NMR Assign. 2016 Apr;10(1):135-8. doi: 10.1007/s12104-015-9652-9. Epub 2015 Oct 19.

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.

Keywords: Drug discovery; NMR; ParE; Resonance assignment; Topoisomerase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anti-Bacterial Agents / pharmacology
  • DNA Topoisomerase IV / chemistry*
  • DNA Topoisomerase IV / metabolism
  • Drug Discovery
  • Escherichia coli / drug effects
  • Escherichia coli / enzymology*
  • Nuclear Magnetic Resonance, Biomolecular*
  • Protein Structure, Secondary
  • Protein Subunits / chemistry*
  • Protein Subunits / metabolism

Substances

  • Anti-Bacterial Agents
  • Protein Subunits
  • DNA Topoisomerase IV