5i4c
From Proteopedia
Crystal structure of non-phosphorylated receiver domain of the stress response regulator RcsB from Escherichia coli
Structural highlights
FunctionRCSB_ECOLI Component of the Rcs signaling system, which controls transcription of numerous genes. RcsB is the response regulator that binds to regulatory DNA regions. Can function both in an RcsA-dependent or RcsA-independent manner. The system regulates expression of numerous genes, including genes involved in colanic acid capsule synthesis, biofilm formation, cell division and outer membrane proteins synthesis. Also involved, with GadE, in control of glutamate-dependent acid resistance, and, with BglJ, in derepression of the cryptic bgl operon. The RcsB-BglJ activity is probably independent of RcsB phosphorylation.[HAMAP-Rule:MF_00981][1] [2] [3] [4] [5] [6] [7] Publication Abstract from PubMedRcsB, 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 non-phosphorylated state. The structure reveals important molecular details of phosphorylation-independent dimerization of RcsB and has implication for the formation of heterodimers. This article is protected by copyright. All rights reserved. Crystal structure of non-phosphorylated receiver domain of the stress response regulator RcsB from Escherichia coli.,Filippova EV, Wawrzak Z, Ruan J, Pshenychnyi S, Schultz RM, Wolfe AJ, Anderson WF Protein Sci. 2016 Sep 27. doi: 10.1002/pro.3050. PMID:27670836[8] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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