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Crystal structure of nonphosphorylated receiver domain of the stress response regulator RcsB from Escherichia coli
Author(s) -
Filippova Ekaterina V.,
Wawrzak Zdzislaw,
Ruan Jiapeng,
Pshenychnyi Sergii,
Schultz Richard M.,
Wolfe Alan J.,
Anderson Wayne F.
Publication year - 2016
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.3050
Subject(s) - protein data bank (rcsb pdb) , response regulator , transcription factor , regulator , biology , dimer , protein data bank , phosphorylation , protein structure , transcription (linguistics) , microbiology and biotechnology , signal transduction , biochemistry , genetics , chemistry , bacteria , gene , bacterial protein , linguistics , philosophy , organic chemistry
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.