ArticleStructure (London, England : 1993)2005
Mechanism of activation for transcription factor PhoB suggested by different modes of dimerization in the inactive and active states.
Article in Structure (London, England : 1993), 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers.
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86 citing papers in PubMed, 141 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
- Article
- PhoU interaction with the PhoR PAS domain is required for repression of the pho regulon and Salmonella virulence, but not for polyphosphate accumulation.Journal of microbiology (Seoul, Korea) · 2025Article
- Untangling the Complexity of Two-Component Signal Transduction in Bacteria.Microorganisms · 2025Review
- Two-Component System Sensor Kinase Inhibitors Target the ATP-Lid of PmrB to Disrupt Colistin Resistance inBiochemistry · 2025Article
- Small DUF1127 proteins regulate bacterial phosphate metabolism through protein-protein interactions with the sensor kinase PhoR.microLife · 2025Article
- An intracellular phosphorus-starvation signal activates the PhoB/PhoR two-component system inmBio · 2024Article
- Multifaceted regulation of siderophore synthesis by multiple regulatory systems in Shewanella oneidensis.Communications biology · 2024Article
- Analysis of CenKR essentiality in Sinorhizobium meliloti and its activity at a target gene promoter in vivo.FEMS microbiology letters · 2024Article
- Chemical Reaction Models in Synthetic Promoter Design in Bacteria.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Phosphorus starvation response and PhoB-independent utilization of organic phosphate sources byMicrobiology spectrum · 2023Article
- Structure of phosphorylated-like RssB, the adaptor delivering σThe Journal of biological chemistry · 2023Article
- Substrate DNA Promoting Binding ofMicroorganisms · 2023Article
- Structural features discriminating hybrid histidine kinase Rec domains from response regulator homologs.Nature communications · 2023Article
- The structural mechanism for transcription activation by Caulobacter crescentus GcrA.Nucleic acids research · 2023Article
- A Copper-Responsive Two-Component System Governs Lipoprotein Remodeling in Listeria monocytogenes.Journal of bacteriology · 2023Article
- Acinetobacter baumannii Regulates Its Stress Responses via the BfmRS Two-Component Regulatory System.Journal of bacteriology · 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
- Coordination of Phosphate and Magnesium Metabolism in Bacteria.Advances in experimental medicine and biology · 2022Article
- Structures of full-length VanR from Streptomyces coelicolor in both the inactive and activated states.Acta crystallographica. Section D, Structural biology · 2021Article
26 more citing papers are in PubMed but not listed here.
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4 authors at 2 institutions in 1 country.
Funding
Abstract
Response regulators (RRs), which undergo phosphorylation/dephosphorylation at aspartate residues, are highly prevalent in bacterial signal transduction. RRs typically contain an N-terminal receiver domain that regulates the activities of a C-terminal DNA binding domain in a phosphorylation-dependent manner. We present crystallography and solution NMR data for the receiver domain of Escherichia coli PhoB which show distinct 2-fold symmetric dimers in the inactive and active states. These structures, together with the previously determined structure of the C-terminal domain of PhoB bound to DNA, define the conformation of the active transcription factor and provide a model for the mechanism of activation in the OmpR/PhoB subfamily, the largest group of RRs. In the active state, the receiver domains dimerize with 2-fold rotational symmetry using their alpha4-beta5-alpha5 faces, while the effector domains bind to DNA direct repeats with tandem symmetry, implying a loss of intramolecular interactions.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.