ArticlePLoS pathogens2017
Structural basis of Zn(II) induced metal detoxification and antibiotic resistance by histidine kinase CzcS in Pseudomonas aeruginosa.
Article in PLoS pathogens, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 31 citations in OpenAlex.
- The two-component system ColRS discriminates metal signals to regulate virulence and resistance in Pseudomonas aeruginosa.PLoS pathogens · 2026Article
- Molecular determinants associated with resistance to imipenem and imipenem-relebactam in clinical Pseudomonas aeruginosa isolates.BMC genomics · 2026Article
- A periplasmic metallochaperone (PmcY) couples ZnAntimicrobial agents and chemotherapy · 2026Article
- Analysis of Putative CzcR Targets Under Zinc Sufficiency and Zinc Excess Conditions inMicroorganisms · 2026Article
- Mechanism ofApplied and environmental microbiology · 2025Article
- A Designed ZnJournal of the American Chemical Society · 2025Article
- Metal-regulated antibiotic resistance and its implications for antibiotic therapy.Microbial biotechnology · 2024Review
- Activation of CzcS/CzcR during zinc excess regulates copper tolerance and pyochelin biosynthesis ofApplied and environmental microbiology · 2024Article
- A type I-F CRISPRi system unveils the novel role of CzcR in modulating multidrug resistance ofMicrobiology spectrum · 2023Article
- Zinc homeostasis in Pseudomonas.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2023Review
- CzcR Is Essential for Swimming Motility in Pseudomonas aeruginosa during Zinc Stress.Microbiology spectrum · 2022Article
- Targeting the Holy Triangle of Quorum Sensing, Biofilm Formation, and Antibiotic Resistance in Pathogenic Bacteria.Microorganisms · 2022Review
- Identification of differentially expressed genes for Pseudomonas sp. Cr13 stimulated by hexavalent chromium.PloS one · 2022Article
- Phylogenetic Analysis with Prediction of Cofactor or Ligand Binding for Pseudomonas aeruginosa PAS and Cache Domains.Microbiology spectrum · 2021Article
- The Connection between Czc and Cad Systems Involved in Cadmium Resistance inInternational journal of molecular sciences · 2021Article
- The requirement for cobalt in vitamin BBiochimica et biophysica acta. Molecular cell research · 2021Review
- The CzcCBA Efflux System Requires the CadA P-Type ATPase for Timely Expression Upon Zinc Excess inFrontiers in microbiology · 2020Article
- DNA-Binding and Transcription Activation by Unphosphorylated Response Regulator AgrR FromFrontiers in microbiology · 2020Article
- CusS-CusR Two-Component System Mediates Tigecycline Resistance in Carbapenem-ResistantFrontiers in microbiology · 2019Article
- Functional Mechanism of the Efflux Pumps Transcription Regulators FromFrontiers in molecular biosciences · 2018Review
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pseudomonas aeruginosa (P. aeruginosa) is a major opportunistic human pathogen, causing serious nosocomial infections among immunocompromised patients by multi-determinant virulence and high antibiotic resistance. The CzcR-CzcS signal transduction system in P. aeruginosa is primarily involved in metal detoxification and antibiotic resistance through co-regulating cross-resistance between Zn(II) and carbapenem antibiotics. Although the intracellular regulatory pathway is well-established, the mechanism by which extracellular sensor domain of histidine kinase (HK) CzcS responds to Zn(II) stimulus to trigger downstream signal transduction remains unclear. Here we determined the crystal structure of the CzcS sensor domain (CzcS SD) in complex with Zn(II) at 1.7 Å resolution. This is the first three-dimensional structural view of Zn(II)-sensor domain of the two-component system (TCS). The CzcS SD is of α/β-fold in nature, and it senses the Zn(II) stimulus at micromole level in a tetrahedral geometry through its symmetry-related residues (His55 and Asp60) on the dimer interface. Though the CzcS SD resembles the PhoQ-DcuS-CitA (PDC) superfamily member, it interacts with the effector in a novel domain with the N-terminal α-helices rather than the conserved β-sheets pocket. The dimerization of the N-terminal H1 and H1' α-helices is of primary importance for the activity of HK CzcS. This study provides preliminary insight into the molecular mechanism of Zn(II) sensing and signaling transduction by the HK CzcS, which will be beneficial to understand how the pathogen P. aeruginosa resists to high levels of heavy metals and antimicrobial agents.
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