ArticleJournal of molecular biology2005
Structural analysis and solution studies of the activated regulatory domain of the response regulator ArcA: a symmetric dimer mediated by the alpha4-beta5-alpha5 face.
Article in Journal of molecular biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.
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Who cites it
84 citing papers in PubMed.
- The protein-water H-bond network for bacterial response regulator REC domain activation.Journal of structural biology: X · 2026Article
- Phosphorylation by the PknB Serine/Threonine Kinase Stimulates Dimer Formation by WalR.Biochemistry · 2026Article
- Constitutive activation of a hybrid two-component regulator reveals cross-regulation of polysaccharide utilization genes in Bacteroides.The Journal of biological chemistry · 2026Article
- Molecular characterization of covRS mutations in M1FEBS open bio · 2026Article
- Historical contingency limits adaptive diversification in a spatially structured environment.Evolution letters · 2026Article
- A novel insight into ComE-mediated activation of gene expression inMicrobiology spectrum · 2025Article
- Non-Canonical Inter-Protein Interactions of Key Proteins Belonging to Cytokinin Signaling Pathways.Plants (Basel, Switzerland) · 2025Review
- A phosphorylation signal activates genome-wide transcriptional control by BfmR, the global regulator of Acinetobacter resistance and virulence.Nucleic acids research · 2025Article
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- A phosphorylation signal activates genome-wide transcriptional control by BfmR, the global regulator ofbioRxiv : the preprint server for biology · 2024Article
- Substrate DNA Promoting Binding ofMicroorganisms · 2023Article
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- The pathogenic mechanism of Mycobacterium tuberculosis: implication for new drug development.Molecular biomedicine · 2022Review
- The ArcAB Two-Component System: Function in Metabolism, Redox Control, and Infection.Microbiology and molecular biology reviews : MMBR · 2022Review
- Thiol redox switches regulate the oligomeric state of cyanobacterial Rre1, RpaA and RpaB response regulators.FEBS letters · 2022Article
- Structure of the Acinetobacter baumannii PmrA receiver domain and insights into clinical mutants affecting DNA binding and promoting colistin resistance.Journal of biochemistry · 2022Article
- Thiol-based functional mimicry of phosphorylation of the two-component system response regulator ArcA promotes pathogenesis in enteric pathogens.Cell reports · 2021Article
- Antibacterial Peptides Resistance inGenes · 2021Review
- Structures of full-length VanR from Streptomyces coelicolor in both the inactive and activated states.Acta crystallographica. Section D, Structural biology · 2021Article
- New Insights into Multistep-Phosphorelay (MSP)/ Two-Component System (TCS) Regulation: Are Plants and Bacteria that Different?Plants (Basel, Switzerland) · 2019Review
24 more citing papers are in PubMed but not listed here.
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3 authors.
Funding
Abstract
Escherichia coli react to changes from aerobic to anaerobic conditions of growth using the ArcA-ArcB two-component signal transduction system. This system, in conjunction with other proteins, regulates the respiratory metabolic pathways in the organism. ArcA is a member of the OmpR/PhoB subfamily of response regulator transcription factors that are known to regulate transcription by binding in tandem to target DNA direct repeats. It is still unclear in this subfamily how activation by phosphorylation of the regulatory domain of response regulators stimulates DNA binding by the effector domain and how dimerization and domain orientation, as well as intra- and intermolecular interactions, affect this process. In order to address these questions we have solved the crystal structures of the regulatory domain of ArcA in the presence and absence of the phosphoryl analog, BeF3-. In the crystal structures, the regulatory domain of ArcA forms a symmetric dimer mediated by the alpha4-beta5-alpha5 face of the protein and involving a number of residues that are highly conserved in the OmpR/PhoB subfamily. It is hypothesized that members of this subfamily use a common mechanism of regulation by dimerization. Additional biophysical studies were employed to probe the oligomerization state of ArcA, as well as its individual domains, in solution. The solution studies show the propensity of the individual domains to associate into oligomers larger than the dimer observed for the intact protein, and suggest that the C-terminal DNA-binding domain also plays a role in oligomerization.
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