ArticleThe Journal of biological chemistry2013
Structural basis of a physical blockage mechanism for the interaction of response regulator PmrA with connector protein PmrD from Klebsiella pneumoniae.
Article in The Journal of biological chemistry, 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.
- Molecular Characteristics and Quantitative Proteomic Analysis ofAntibiotics (Basel, Switzerland) · 2022Article
- Regulating polymyxin resistance in Gram-negative bacteria: roles of two-component systems PhoPQ and PmrAB.Future microbiology · 2020Review
- Multifaceted mechanisms of colistin resistance revealed by genomic analysis of multidrug-resistant Klebsiella pneumoniae isolates from individual patients before and after colistin treatment.The Journal of infection · 2019Article
- Colistin heteroresistance in Enterobacter cloacae is regulated by PhoPQ-dependent 4-amino-4-deoxy-l-arabinose addition to lipid A.Molecular microbiology · 2019Article
- Two Component Regulatory Systems and Antibiotic Resistance in Gram-Negative Pathogens.International journal of molecular sciences · 2019Review
- Crystal structure of nonphosphorylated receiver domain of the stress response regulator RcsB from Escherichia coli.Protein science : a publication of the Protein Society · 2016Article
- Amino Acid Substitutions of CrrB Responsible for Resistance to Colistin through CrrC in Klebsiella pneumoniae.Antimicrobial agents and chemotherapy · 2016Article
- Structure and dynamics of polymyxin-resistance-associated response regulator PmrA in complex with promoter DNA.Nature communications · 2015Article
- PmrD is required for modifications to escherichia coli endotoxin that promote antimicrobial resistance.Antimicrobial agents and chemotherapy · 2015Article
- Genomic and transcriptomic analyses of colistin-resistant clinical isolates of Klebsiella pneumoniae reveal multiple pathways of resistance.Antimicrobial agents and chemotherapy · 2015Article
- Solution structure and tandem DNA recognition of the C-terminal effector domain of PmrA from Klebsiella pneumoniae.Nucleic acids research · 2014Article
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
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 Fe(3+) 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 (PmrA(N)) 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-PmrA(N), 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.
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