ArticleThe Journal of biological chemistry2013
The structure of Bradyrhizobium japonicum transcription factor FixK2 unveils sites of DNA binding and oxidation.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 28 citations in OpenAlex.
- Article
- A Structure-Based Analysis of the Evolution of Transcription Factors of the FNR/CRP Family.Biomolecules · 2026Review
- 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
- Surface Plasmon Resonance as a Tool to Elucidate the Molecular Determinants of Key Transcriptional Regulators Controlling Rhizobial Lifestyles.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Bradyrhizobium ottawaense efficiently reduces nitrous oxide through high nosZ gene expression.Scientific reports · 2023Article
- Development of in-line anoxic small-angle X-ray scattering and structural characterization of an oxygen-sensing transcriptional regulator.bioRxiv : the preprint server for biology · 2023Article
- Structural and functional diversity of bacterial cyclic nucleotide perception by CRP proteins.microLife · 2023Review
- Fine-Tuning Modulation of Oxidation-Mediated Posttranslational Control ofInternational journal of molecular sciences · 2022Article
- Role of Regulated Proteolysis in the Communication of Bacteria With the Environment.Frontiers in molecular biosciences · 2020Review
- Expanding the Regulon of theFrontiers in microbiology · 2019Article
- Reassessing the Structure and Function Relationship of the OAntioxidants & redox signaling · 2018Review
- Mismodeled purines: implicit alternates and hidden Hoogsteens.Acta crystallographica. Section D, Structural biology · 2017Article
- FixKFrontiers in microbiology · 2017Article
- Structural basis for glutathione-mediated activation of the virulence regulatory protein PrfA in Listeria.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Nitrogen Fixation and Molecular Oxygen: Comparative Genomic Reconstruction of Transcription Regulation in Alphaproteobacteria.Frontiers in microbiology · 2016Article
- The crystal structure of the global anaerobic transcriptional regulator FNR explains its extremely fine-tuned monomer-dimer equilibrium.Science advances · 2015Article
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6 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
FixK2 is a regulatory protein that activates a large number of genes for the anoxic and microoxic, endosymbiotic, and nitrogen-fixing life styles of the α-proteobacterium Bradyrhizobium japonicum. FixK2 belongs to the cAMP receptor protein (CRP) superfamily. Although most CRP family members are coregulated by effector molecules, the activity of FixK2 is negatively controlled by oxidation of its single cysteine (Cys-183) located next to the DNA-binding domain and possibly also by proteolysis. Here, we report the three-dimensional x-ray structure of FixK2, a representative of the FixK subgroup of the CRP superfamily. Crystallization succeeded only when (i) an oxidation- and protease-insensitive protein variant (FixK2(C183S)-His6) was used in which Cys-183 was replaced with serine and the C terminus was fused with a hexahistidine tag and (ii) this protein was allowed to form a complex with a 30-mer double-stranded target DNA. The structure of the FixK2-DNA complex was solved at a resolution of 1.77 Å, at which the protein formed a homodimer. The precise protein-DNA contacts were identified, which led to an affirmation of the canonical target sequence, the so-called FixK2 box. The C terminus is surface-exposed, which might explain its sensitivity to specific cleavage and degradation. The oxidation-sensitive Cys-183 is also surface-exposed and in close proximity to DNA. Therefore, we propose a mechanism whereby the oxo acids generated after oxidation of the cysteine thiol cause an electrostatic repulsion, thus preventing specific DNA binding.
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