ArticleProtein science : a publication of the Protein Society2013
The dimeric form of the unphosphorylated response regulator BaeR.
Article in Protein science : a publication of the Protein Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 15 citations in OpenAlex.
- Constitutive activation of a hybrid two-component regulator reveals cross-regulation of polysaccharide utilization genes in Bacteroides.The Journal of biological chemistry · 2026Article
- Exploration of Phosphoproteins inPathogens (Basel, Switzerland) · 2025Article
- Repurposing FDA-approved drugs for combating tigecycline resistance in Acinetobacter baumannii: in silico screening against BaeR protein.Molecular diversity · 2025Article
- Article
- Structures of full-length VanR from Streptomyces coelicolor in both the inactive and activated states.Acta crystallographica. Section D, Structural biology · 2021Article
- Epistatic Effect of Regulators to the Adaptive Growth of Escherichia coli.Scientific reports · 2020Article
- Can I solve my structure by SAD phasing? Planning an experiment, scaling data and evaluating the useful anomalous correlation and anomalous signal.Acta crystallographica. Section D, Structural biology · 2016Article
- Structure of the Response Regulator NsrR from Streptococcus agalactiae, Which Is Involved in Lantibiotic Resistance.PloS one · 2016Article
- Overexpression, purification and crystallization of the response regulator NsrR involved in nisin resistance.Acta crystallographica. Section F, Structural biology communications · 2015Article
- Article
- A response regulator from a soil metagenome enhances resistance to the β-lactam antibiotic carbenicillin in Escherichia coli.PloS one · 2015Article
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial response regulators (RRs) can regulate the expression of genes that confer antibiotic resistance; they contain a receiver and an effector domain and their ability to bind DNA is based on the dimerization state. This is triggered by phosphorylation of the receiver domain by a kinase. However, even in the absence of phosphorylation RRs can exist in equilibrium between monomers and dimers with phosphorylation shifting the equilibrium toward the dimer form. We have determined the crystal structure of the unphosphorylated dimeric BaeR from Escherichia coli. The dimer interface is formed by a domain swap at the receiver domain. In comparison with the unphosphorylated dimeric PhoP from Mycobacterium tuberculosis, BaeR displays an asymmetry of the effector domains.
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