ArticleScientific reports2016
Structural Analysis of the Hg(II)-Regulatory Protein Tn501 MerR from Pseudomonas aeruginosa.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 51 citations in OpenAlex.
- Probe-based identification of metal-binding sites using deep learning representations.Nature communications · 2026Article
- Metals in Motion: Understanding Labile Metal Pools in Bacteria.Biochemistry · 2025Review
- Bacterial Metallostasis: Metal Sensing, Metalloproteome Remodeling, and Metal Trafficking.Chemical reviews · 2024Review
- Article
- Determinants ofGenes · 2024Article
- CvkR is a MerR-type transcriptional repressor of class 2 type V-K CRISPR-associated transposase systems.Nature communications · 2023Article
- The protein scaffold calibrates metal specificity and activation in MerR sensors.Microbial biotechnology · 2022Article
- Bacterial MerR family transcription regulators: activationby distortion.Acta biochimica et biophysica Sinica · 2022Review
- A study on the secondary structure of the metalloregulatory protein CueR: effect of pH, metal ions and DNA.European biophysics journal : EBJ · 2021Article
- Potential Whole-Cell Biosensors for Detection of Metal Using MerR Family Proteins fromMicromachines · 2021Article
- Flexibility of the CueR Metal Site Probed by Instantaneous Change of Element and Oxidation State from AgChemistry (Weinheim an der Bergstrasse, Germany) · 2020Article
- Selective cadmium regulation mediated by a cooperative binding mechanism in CadR.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- The Response ofFrontiers in microbiology · 2019Article
- The MerR-like protein BldC binds DNA direct repeats as cooperative multimers to regulate Streptomyces development.Nature communications · 2018Article
Corrections and comments
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Authors and funding
11 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The metalloprotein MerR is a mercury(II)-dependent transcriptional repressor-activator that responds to mercury(II) with extraordinary sensitivity and selectivity. It's widely distributed in both Gram-negative and Gram-positive bacteria but with barely detectable sequence identities between the two sources. To provide structural basis for the considerable biochemical and biophysical experiments previously performed on Tn501 and Tn21 MerR from Gram-negative bacteria, we analyzed the crystal structure of mercury(II)-bound Tn501 MerR. The structure in the metal-binding domain provides Tn501 MerR with a high affinity for mercury(II) and the ability to distinguish mercury(II) from other metals with its unique planar trigonal coordination geometry, which is adopted by both Gram-negative and Gram-positive bacteria. The mercury(II) coordination state in the C-terminal metal-binding domain is transmitted through the allosteric network across the dimer interface to the N-terminal DNA-binding domain. Together with the previous mutagenesis analyses, the present data indicate that the residues in the allosteric pathway have a central role in maintaining the functions of Tn501 MerR. In addition, the complex structure exhibits significant differences in tertiary and quaternary structural arrangements compared to those of Bacillus MerR from Gram-positive bacteria, which probably enable them to function with specific promoter DNA with different spacers between -35 and -10 elements.
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