ArticleBiochemistry2013
Roles of the A and C sites in the manganese-specific activation of MntR.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
32 citing papers in PubMed, 42 citations in OpenAlex.
- Microbial metal physiology: ions to ecosystems.Nature reviews. Microbiology · 2025Review
- Structural basis for transcription activation through cooperative recruitment of MntR.Nature communications · 2025Article
- Bacterial Metallostasis: Metal Sensing, Metalloproteome Remodeling, and Metal Trafficking.Chemical reviews · 2024Review
- A riboswitch-controlled TerC family transporter Alx tunes intracellular manganese concentration inJournal of bacteriology · 2024Article
- A water-soluble, cell-permeable Mn(ii) sensor enables visualization of manganese dynamics in live mammalian cells.Chemical science · 2024Article
- Small-Molecule Fluorescent Probes for Binding- and Activity-Based Sensing of Redox-Active Biological Metals.Chemical reviews · 2024Review
- Fluorescent Protein-Based Sensors for Detecting Essential Metal Ions across the Tree of Life.ACS sensors · 2024Review
- Structural Dynamics of theInternational journal of molecular sciences · 2023Article
- Why is manganese so valuable to bacterial pathogens?Frontiers in cellular and infection microbiology · 2023Review
- Iron homeostasis inMicrobiology (Reading, England) · 2023Article
- A genetically encoded fluorescent sensor for manganese(II), engineered from lanmodulin.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Genetic Regulation of Metal Ion Homeostasis in Staphylococcus aureus.Trends in microbiology · 2020Review
- Metalation: nature's challenge in bioinorganic chemistry.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020Review
- Exploring the Specificity of Rationally Designed Peptides Reconstituted from the Cell-Free Extract ofInorganic chemistry · 2020Article
- Allosteric control of metal-responsive transcriptional regulators in bacteria.The Journal of biological chemistry · 2020Review
- Structural analysis of the manganese transport regulator MntR from Bacillus halodurans in apo and manganese bound forms.PloS one · 2019Article
- Redox Sensing by FeAntioxidants & redox signaling · 2018Review
- Convergent Use of Heptacoordination for Cation Selectivity by RNA and Protein Metalloregulators.Cell chemical biology · 2018Article
- Metal homeostasis and resistance in bacteria.Nature reviews. Microbiology · 2017Review
- Metallochaperones and metalloregulation in bacteria.Essays in biochemistry · 2017Review
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
Abstract
The manganese transport regulator (MntR) represses the expression of genes involved in manganese uptake in Bacillus subtilis. It selectively responds to Mn(2+) and Cd(2+) over other divalent metal cations, including Fe(2+), Co(2+), and Zn(2+). Previous work has shown that MntR forms binuclear complexes with Mn(2+) or Cd(2+) at two binding sites, labeled A and C, that are separated by 4.4 Å. Zinc activates MntR poorly and binds only to the A site, forming a mononuclear complex. The difference in metal binding stoichiometry suggested a mechanism for selectivity in MntR. Larger metal cations are strongly activating because they can form the binuclear complex, while smaller metal ions cannot bind with the geometry needed to fully occupy both metal binding sites. To investigate this hypothesis, structures of MntR in complex with two other noncognate metal ions, Fe(2+) and Co(2+), have been determined. Each metal forms a mononuclear complex with MntR with the metal ion bound in the A site, supporting the conclusions drawn from the Zn(2+) complex. Additionally, we investigated two site-specific mutants of MntR, E11K and H77A, that contain substitutions of metal binding residues in the A site. While metal binding in each mutant is significantly altered relative to that of wild-type MntR, both mutants retain activity and selectivity for Mn(2+) in vitro and in vivo. That observation, coupled with previous studies, suggests that the A and C sites both contribute to the selectivity of MntR.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.