ArticleProtein science : a publication of the Protein Society2016
Crystal structure of nonphosphorylated receiver domain of the stress response regulator RcsB from Escherichia coli.
Article in Protein science : a publication of the Protein Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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6 citing papers in PubMed, 10 citations in OpenAlex.
- Binding site profiles and N-terminal minor groove interactions of the master quorum-sensing regulator LuxR enable flexible control of gene activation and repression.Nucleic acids research · 2021Article
- Structure-based analyses of Salmonella RcsB variants unravel new features of the Rcs regulon.Nucleic acids research · 2021Article
- Article
- Conformational dynamism for DNA interaction in the Salmonella RcsB response regulator.Nucleic acids research · 2018Article
- Involvement of Two-Component Signaling on Bacterial Motility and Biofilm Development.Journal of bacteriology · 2017Review
- New Insights into the Non-orthodox Two Component Rcs Phosphorelay System.Frontiers in microbiology · 2017Review
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
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.
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