ArticleScience advances2015
The crystal structure of the global anaerobic transcriptional regulator FNR explains its extremely fine-tuned monomer-dimer equilibrium.
Article in Science advances, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 51 citations in OpenAlex.
- EnterotoxigenicProceedings of the National Academy of Sciences of the United States of America · 2018Trial
- An interfacial-intramolecular electron highway for accelerated electrocatalytic CONature communications · 2026Article
- A Structure-Based Analysis of the Evolution of Transcription Factors of the FNR/CRP Family.Biomolecules · 2026Review
- From environmental signals to adaptive phenotypes: signal-responsive regulation and network logic of bacterial small RNAs.FEMS microbiology reviews · 2026Review
- ArnR binds a [4Fe-4S] cluster and indirectly senses anaerobicity in Corynebacteria.Metallomics : integrated biometal science · 2025Article
- Archaeal protein containing domain of unknown function 2193 undergoes oligomeric reconfiguration upon iron-sulfur cluster binding.FEBS letters · 2025Article
- Structurally diverse C-terminal accessory domains in type I ABC importers reveal distinct regulatory mechanisms.Structure (London, England : 1993) · 2025Review
- Engineering the Escherichia coli Nissle strain for monitoring the bacterial cell distribution and therapeutic protein expression within the intestinal tract of animal models.Biotechnology letters · 2025Article
- Structures of the cyanobacterial nitrogen regulators NtcA and PipX complexed to DNA shed light on DNA binding by NtcA and implicate PipX in the recruitment of RNA polymerase.Nucleic acids research · 2025Article
- Structural determinants of DNA recognition by the NO sensor NsrR and related Rrf2-type [FeS]-transcription factors.Communications biology · 2022Article
- Iron-sulfur clusters as inhibitors and catalysts of viral replication.Nature chemistry · 2022Review
- A conserved and seemingly redundant Escherichia coli biotin biosynthesis gene expressed only during anaerobic growth.Molecular microbiology · 2021Article
- Bacterial approaches to sensing and responding to respiration and respiration metabolites.Molecular microbiology · 2021Review
- Construction of a sustainable 3-hydroxybutyrate-producing probiotic Escherichia coli for treatment of colitis.Cellular & molecular immunology · 2021Article
- FNR-Type Regulator GoxR of the Obligatorily Aerobic Acetic Acid BacteriumApplied and environmental microbiology · 2021Article
- The Central Role of Redox-Regulated Switch Proteins in Bacteria.Frontiers in molecular biosciences · 2021Review
- Interactions among Redox Regulators and the CtrA Phosphorelay inMicroorganisms · 2020Article
- Structural basis of non-canonical transcriptional regulation by the σA-bound iron-sulfur protein WhiB1 in M. tuberculosis.Nucleic acids research · 2020Article
- Identification and Unusual Properties of the Master Regulator FNR in the Extreme AcidophileFrontiers in microbiology · 2019Article
- Reassessing the Structure and Function Relationship of the OAntioxidants & redox signaling · 2018Review
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The structure of the dimeric holo-fumarate and nitrate reduction regulator (FNR) from Aliivibrio fischeri has been solved at 2.65 Å resolution. FNR globally controls the transition between anaerobic and aerobic respiration in facultative anaerobes through the assembly/degradation of its oxygen-sensitive [4Fe-4S] cluster. In the absence of O2, FNR forms a dimer and specifically binds to DNA, whereas in its presence, the cluster is degraded causing FNR monomerization and DNA dissociation. We have used our crystal structure and the information previously gathered from numerous FNR variants to propose that this process is governed by extremely fine-tuned interactions, mediated by two salt bridges near the amino-terminal cluster-binding domain and an "imperfect" coiled-coil dimer interface. [4Fe-4S] to [2Fe-2S] cluster degradation propagates a conformational signal that indirectly causes monomerization by disrupting the first of these interactions and unleashing the "unzipping" of the FNR dimer in the direction of the carboxyl-terminal DNA binding domain.
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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.