5I4C

Crystal structure of non-phosphorylated receiver domain of the stress response regulator RcsB from Escherichia coli

Summary for 5I4C

• Entry DOI: 10.2210/pdb5i4c/pdb
• Descriptor: Transcriptional regulatory protein RcsB (2 entities in total)
• Functional Keywords: rcs phosphorelay, dna-binding, transcriptional regulator, rpra, structural genomics, csgid, center for structural genomics of infectious diseases, hydrolase, gene regulation
• Biological source: Escherichia coli (strain K12)
• Total number of polymer chains: 1
• Total formula weight: 16037.64

Authors

Filippova, E.V.,Wawrzak, Z.,Minasov, G.,Ruan, J.,Pshenychnyi, S.,Wolfe, A.J.,Anderson, W.F.,Center for Structural Genomics of Infectious Diseases (CSGID) (deposition date: 2016-02-11, release date: 2016-10-12, Last modification date: 2024-03-06)

Primary citation

Filippova, E.V.,Wawrzak, Z.,Ruan, J.,Pshenychnyi, S.,Schultz, R.M.,Wolfe, A.J.,Anderson, W.F.
Crystal structure of nonphosphorylated receiver domain of the stress response regulator RcsB from Escherichia coli.
Protein Sci., 25:2216-2224, 2016

PubMed 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.

PubMed: 27670836
DOI: 10.1002/pro.3050

Experimental method

X-RAY DIFFRACTION (2 Å)