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• W2030431683 abstract "In bacteria, the two-component system is the most prevalent for sensing and transducing environmental signals into the cell. The PmrA-PmrB two-component system, responsible for sensing external stimuli of high Fe3+ and mild acidic conditions, can control the genes involved in lipopolysaccharide modification and polymyxin resistance in pathogens. In Klebsiella pneumoniae, the small basic connector protein PmrD protects phospho-PmrA and prolongs the expression of PmrA-activated genes. We previously determined the phospho-PmrA recognition mode of PmrD. However, how PmrA interacts with PmrD and prevents its dephosphorylation remains unknown. To address this question, we solved the x-ray crystal structure of the N-terminal receiver domain of BeF3−-activated PmrA (PmrAN) at 1.70 Å. With this structure, we applied the data-driven docking method based on NMR chemical shift perturbation to generate the complex model of PmrD-PmrAN, which was further validated by site-directed spin labeling experiments. In the complex model, PmrD may act as a blockade to prevent phosphatase from contacting with the phosphorylation site on PmrA.Background: PmrD binds to phospho-PmrA and sustains its phosphorylation state.Results: Phospho-PmrA interacts with PmrD via several specific intermolecular interactions.Conclusion: A steric inhibition mechanism was proposed for protecting phospho-PmrA against dephosphorylation.Significance: This work provides novel data revealing how a connector protein protects an activated response regulator. In bacteria, the two-component system is the most prevalent for sensing and transducing environmental signals into the cell. The PmrA-PmrB two-component system, responsible for sensing external stimuli of high Fe3+ and mild acidic conditions, can control the genes involved in lipopolysaccharide modification and polymyxin resistance in pathogens. In Klebsiella pneumoniae, the small basic connector protein PmrD protects phospho-PmrA and prolongs the expression of PmrA-activated genes. We previously determined the phospho-PmrA recognition mode of PmrD. However, how PmrA interacts with PmrD and prevents its dephosphorylation remains unknown. To address this question, we solved the x-ray crystal structure of the N-terminal receiver domain of BeF3−-activated PmrA (PmrAN) at 1.70 Å. With this structure, we applied the data-driven docking method based on NMR chemical shift perturbation to generate the complex model of PmrD-PmrAN, which was further validated by site-directed spin labeling experiments. In the complex model, PmrD may act as a blockade to prevent phosphatase from contacting with the phosphorylation site on PmrA. Background: PmrD binds to phospho-PmrA and sustains its phosphorylation state. Results: Phospho-PmrA interacts with PmrD via several specific intermolecular interactions. Conclusion: A steric inhibition mechanism was proposed for protecting phospho-PmrA against dephosphorylation. Significance: This work provides novel data revealing how a connector protein protects an activated response regulator." @default.
• W2030431683 created "2016-06-24" @default.
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• W2030431683 date "2013-08-01" @default.
• W2030431683 modified "2023-10-17" @default.
• W2030431683 title "Structural Basis of a Physical Blockage Mechanism for the Interaction of Response Regulator PmrA with Connector Protein PmrD from Klebsiella pneumoniae" @default.
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• W2030431683 doi "https://doi.org/10.1074/jbc.m113.481978" @default.
• W2030431683 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3757216" @default.
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