Crystal structure of nonphosphorylated receiver domain of the stress response regulator RcsB from Escherichia coli

Ekaterina V. Filippova*, Zdzislaw Wawrzak, Jiapeng Ruan, Sergii Pshenychnyi, Richard M. Schultz, Alan J. Wolfe, Wayne F. Anderson

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

7 Scopus citations

Abstract

RcsB, the transcription-associated response regulator of the Rcs phosphorelay two-component signal transduction system, activates cell stress responses associated with desiccation, cell wall biosynthesis, cell division, virulence, biofilm formation, and antibiotic resistance in enteric bacterial pathogens. RcsB belongs to the FixJ/NarL family of transcriptional regulators, which are characterized by a highly conserved C-terminal DNA-binding domain. The N-terminal domain of RcsB belongs to the family of two-component receiver domains. This receiver domain contains the phosphoacceptor site and participates in RcsB dimer formation; it also contributes to dimer formation with other transcription factor partners. Here, we describe the crystal structure of the Escherichia coli RcsB receiver domain in its nonphosphorylated state. The structure reveals important molecular details of phosphorylation-independent dimerization of RcsB and has implication for the formation of heterodimers.

Original languageEnglish (US)
Pages (from-to)2216-2224
Number of pages9
JournalProtein Science
Volume25
Issue number12
DOIs
StatePublished - Dec 1 2016

Keywords

  • FixJ/NarL family
  • Rcs phosphorelay
  • phosphorylation domain
  • transcriptional regulator
  • two-component signal transduction system

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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