Unnatural amino acid substitution as a probe of the allosteric coupling pathway in a mycobacterial Cu(I) sensor

Zhen Ma, Darin M. Cowart, Brian P. Ward, Randy J. Arnold, Richard D. DiMarchi, Limei Zhang, Graham N. George, Robert A. Scott, David P. Giedroc

Research output: Contribution to journalArticle

48 Scopus citations

Abstract

(Chemical Equation Presented) The Cu(I) sensor Mycobacterium tuberculosis CsoR is a founding member of a new metalloregulatory protein family. Here we show that two "atom" substitutions of the NB2 face of a Cu(I) coordinating histisine-61 allosterically uncouple Cu(I) and DNA binding, with no effect on Cu(I) binding affinity and coordination structure. A model analogous to the allosteric switch mechanism in Staphylococcus aureus CzrA, a zinc sensor protein with a completely different fold, is proposed.

Original languageEnglish (US)
Pages (from-to)18044-18045
Number of pages2
JournalJournal of the American Chemical Society
Volume131
Issue number50
DOIs
StatePublished - Dec 23 2009

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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    Ma, Z., Cowart, D. M., Ward, B. P., Arnold, R. J., DiMarchi, R. D., Zhang, L., George, G. N., Scott, R. A., & Giedroc, D. P. (2009). Unnatural amino acid substitution as a probe of the allosteric coupling pathway in a mycobacterial Cu(I) sensor. Journal of the American Chemical Society, 131(50), 18044-18045. https://doi.org/10.1021/ja908372b