EPR Spectroscopy Detects Various Active State Conformations of the Transcriptional Regulator CueR

Hila Sameach, Shreya Ghosh, Lada Gevorkyan-Airapetov, Sunil Saxena, Sharon Ruthstein

Research output: Contribution to journalArticlepeer-review

50 Scopus citations


The interactions between proteins and their specific DNA sequences are the basis of many cellular processes. Hence, developing methods to build an atomic level picture of these interactions helps improve our understanding of key cellular mechanisms. CueR is an Escherichia coli copper-sensing transcription regulator. The inhibition of copper-sensing transcription regulators can kill pathogens, without harming the host. Several spectroscopic studies and crystallographic data have suggested that changes in the conformation of both the DNA and the protein control transcription. However, due to the inadequate resolution of these methods, the exact number of active conformations of CueR has not been determined. Resolving the structure of CueR in its active state is highly important for the development of specific inhibitors. Herein, the potential of double-histidine (dHis)-based Cu II spin labeling for the identification of various conformational states of CueR during transcription is shown.

Original languageEnglish
Pages (from-to)3053-3056
Number of pages4
JournalAngewandte Chemie - International Edition
Issue number10
StatePublished - 4 Mar 2019

Bibliographical note

Publisher Copyright:
© 2019 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim


We acknowledge the support of ISF grant no. 176/16 (to S.R.) and NSF MCB-1613007 (to S.S.).

FundersFunder number
National Science FoundationMCB-1613007
Israel Science Foundation176/16


    • DEER
    • EPR spectroscopy
    • copper regulators
    • protein–DNA
    • spin labeling


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