ArticleJournal of bacteriology2011
Structure of the periplasmic stress response protein CpxP.
Article in Journal of bacteriology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 55 citations in OpenAlex.
- The divergentMicrobiology (Reading, England) · 2026Article
- High-level polymyxin B resistance and underlying mechanism in a multidrug-resistant Acinetobacter strain isolated from the marine plastisphere.The Journal of antibiotics · 2026Article
- Transcriptome-guided discovery of novel plant-associated genes in a rhizosphere Pseudomonas.Microbiome · 2025Article
- Repair of oxidized methionine residues in the chaperone Spy maintains periplasmic proteostasis under chlorite stress in Escherichia coli.PLoS biology · 2025Article
- Patterns of Fitness and Gene Expression Epistasis Generated by Beneficial Mutations in the rho and rpoB Genes of Escherichia coli during High-Temperature Adaptation.Molecular biology and evolution · 2024Article
- Stress response in Escherichia coli following sublethal phenalene-1-one mediated antimicrobial photodynamic therapy: an RNA-Seq study.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2024Article
- Cpx-signalling innpj antimicrobials and resistance · 2024Article
- Experimental Evolution of Copper Resistance inAntibiotics (Basel, Switzerland) · 2022Article
- Structural investigation on SPI-6-associated Salmonella typhimurium VirG-like stress protein that promotes pathogen survival in macrophages.Protein science : a publication of the Protein Society · 2022Article
- Article
- Knocking out Analysis of the CpxP gene using Crispr/Cas9 in Escherichia coli MG1655.AMB Express · 2020Article
- High-ResolutionBiochemistry · 2020Article
- Zmo0994, a novel LEA-like protein fromBiotechnology for biofuels · 2020Article
- Periplasmic Chaperones and Prolyl Isomerases.EcoSal Plus · 2018Review
- Envelope Stress Responses: An Interconnected Safety Net.Trends in biochemical sciences · 2017Review
- Global Gene-expression Analysis of the Response ofFrontiers in microbiology · 2017Article
- CpxR Activates MexAB-OprM Efflux Pump Expression and Enhances Antibiotic Resistance in Both Laboratory and Clinical nalB-Type Isolates of Pseudomonas aeruginosa.PLoS pathogens · 2016Article
- The Vibrio cholerae Cpx envelope stress response senses and mediates adaptation to low iron.Journal of bacteriology · 2015Article
- Segmental helical motions and dynamical asymmetry modulate histidine kinase autophosphorylation.PLoS biology · 2014Article
- Dynamic interaction between the CpxA sensor kinase and the periplasmic accessory protein CpxP mediates signal recognition in E. coli.PloS one · 2014Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
CpxP is a novel bacterial periplasmic protein with no homologues of known function. In gram-negative enteric bacteria, CpxP is thought to interact with the two-component sensor kinase, CpxA, to inhibit induction of the Cpx envelope stress response in the absence of protein misfolding. CpxP has also been shown to facilitate DegP-mediated proteolysis of misfolded proteins. Six mutations that negate the ability of CpxP to function as a signaling protein are localized in or near two conserved LTXXQ motifs that define a class of proteins with similarity to CpxP, Pfam PF07813. To gain insight into how these mutations might affect CpxP signaling and/or proteolytic adaptor functions, the crystal structure of CpxP from Escherichia coli was determined to 2.85-Å resolution. The structure revealed an antiparallel dimer of intertwined α-helices with a highly basic concave surface. Each protomer consists of a long, hooked and bent hairpin fold, with the conserved LTXXQ motifs forming two diverging turns at one end. Biochemical studies demonstrated that CpxP maintains a dimeric state but may undergo a slight structural adjustment in response to the inducing cue, alkaline pH. Three of the six previously characterized cpxP loss-of-function mutations, M59T, Q55P, and Q128H, likely result from a destabilization of the protein fold, whereas the R60Q, D61E, and D61V mutations may alter intermolecular interactions.
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