ArticleProceedings of the National Academy of Sciences of the United States of America2006
Atomic structure of a nitrate-binding protein crucial for photosynthetic productivity.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 86 citations in OpenAlex.
- Structure-informed engineering of plant-microbe interactions.The Plant journal : for cell and molecular biology · 2026Review
- Structural basis for the ion selectivity of potassium-chloride cotransporter KCC4 revealed by cryo-EM titration.Biophysics reports · 2026Article
- Genetically Encoded Fluorescent Biosensors Enable Noninvasive Real-Time Visualization of Nitrate Dynamics in Intact Living Plants.Biosensors · 2026Article
- The molecular mechanism of the cyanobacterial bicarbonate importer CmpABCD activated by the intracellular nitrate.Nature communications · 2026Article
- Deciphering guanidine assimilation and riboswitch-based gene regulation in cyanobacteria for synthetic biology applications.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- NitrOFF: An Engineered Fluorescent Biosensor to Illuminate Nitrate Transport in Living Cells.Angewandte Chemie (International ed. in English) · 2025Article
- Diurnal rhythm causes metabolic crises in the cyanobacterial mutants of c-di-AMP signaling cascade.iScience · 2025Article
- Structurally diverse C-terminal accessory domains in type I ABC importers reveal distinct regulatory mechanisms.Structure (London, England : 1993) · 2025Review
- NitrOFF: An engineered fluorescent biosensor to illuminate nitrate transport in living cells.bioRxiv : the preprint server for biology · 2025Article
- Engineering the cyanobacterial ATP-driven BCT1 bicarbonate transporter for functional targeting to C3 plant chloroplasts.Journal of experimental botany · 2024Article
- Allosteric regulation of nitrate transporter NRT via the signaling protein PII.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Locations of membrane protein production in a cyanobacterium.Journal of bacteriology · 2023Article
- Biophysical andChemical communications (Cambridge, England) · 2022Article
- Functional characterisation of substrate-binding proteins to address nutrient uptake in marine picocyanobacteria.Biochemical Society transactions · 2021Review
- Article
- A Fluorescence Resonance Energy Transfer-Based Analytical Tool for Nitrate Quantification in Living Cells.ACS omega · 2020Article
- Carbon/nitrogen homeostasis control in cyanobacteria.FEMS microbiology reviews · 2020Review
- Differential Binding of Tetrel-Bonding Bipodal Receptors to Monatomic and Polyatomic Anions.Molecules (Basel, Switzerland) · 2019Article
- Nitrogen Cycling in Soybean Rhizosphere: Sources and Sinks of Nitrous Oxide (NFrontiers in microbiology · 2019Review
- The Signal Transduction Protein PFrontiers in microbiology · 2019Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cyanobacteria, blue-green algae, are the most abundant autotrophs in aquatic environments and form the base of all aquatic food chains by fixing carbon and nitrogen into cellular biomass. The single most important nutrient for photosynthesis and growth is nitrate, which is severely limiting in many aquatic environments particularly the open ocean. It is therefore not surprising that NrtA, the solute-binding component of the high-affinity nitrate ABC transporter, is the single-most abundant protein in the plasma membrane of these bacteria. Here, we describe the structure of a nitrate-specific receptor, NrtA from Synechocystis sp. PCC 6803, complexed with nitrate and determined to a resolution of 1.5 A. NrtA is significantly larger than other oxyanion-binding proteins, representing a previously uncharacterized class of transport proteins. From sequence alignments, the only other solute-binding protein in this class is CmpA, a bicarbonate-binding protein. Therefore, these organisms created a solute-binding protein for two of the most important nutrients: inorganic nitrogen and carbon. The electrostatic charge distribution of NrtA appears to force the protein off the membrane while the flexible tether facilitates the delivery of nitrate to the membrane pore. The structure not only details the determinants for nitrate selectivity in NrtA but also the bicarbonate specificity in CmpA. Nitrate and bicarbonate transport are regulated by the cytoplasmic proteins NrtC and CmpC, respectively. Interestingly, the residues lining the ligand binding pockets suggest that they both bind nitrate. This implies that the nitrogen and carbon uptake pathways are synchronized by intracellular nitrate and nitrite.
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