期刊
PROTEIN SCIENCE
卷 25, 期 12, 页码 2216-2224出版社
WILEY
DOI: 10.1002/pro.3050
关键词
transcriptional regulator; Rcs phosphorelay; two-component signal transduction system; phosphorylation domain; FixJ/NarL family
资金
- Argonne National Laboratory, University of Chicago Argonne, LLC
- U.S. Department of Energy, Office of Biological and Environmental Research [DE-AC02-06CH11357]
- Michigan Economic Development Corporation
- Michigan Technology Tri-Corridor [085P1000817]
- National Institute of Allergy and Infectious Diseases, National Institutes of Health, Department of Health and Human Services [HHSN272200700058C, HHSN272201200026C]
- Department of Energy [DE-SC0012443]
- National Institutes of Health [2R01AI083640-06A1]
- U.S. Department of Energy (DOE) [DE-SC0012443] Funding Source: U.S. Department of Energy (DOE)
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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