ArticleProceedings of the National Academy of Sciences of the United States of America2010
Mechanism of 2-oxoglutarate signaling by the Synechococcus elongatus PII signal transduction protein.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 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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Who cites it
45 citing papers in PubMed, 111 citations in OpenAlex.
- Article
- PII interactions with the acetyl-CoA carboxylase subunits BADC and BCCP co-regulate lipid and nitrogen metabolism in Arabidopsis.Plant physiology · 2025Article
- 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
- Roles of second messengers in the regulation of cyanobacterial physiology: the carbon-concentrating mechanism and beyond.microLife · 2023Review
- Photoautotrophic Growth Rate Enhancement ofBiology · 2022Article
- Chemoproteomic identification of CONature chemical biology · 2022Article
- Patterning of the Autotrophic, Mixotrophic, and Heterotrophic Proteomes of Oxygen-Evolving CyanobacteriumFrontiers in microbiology · 2022Article
- Split NanoLuc technology allows quantitation of interactions between PII protein and its receptors with unprecedented sensitivity and reveals transient interactions.Scientific reports · 2021Article
- Crystal structures of adenylylated and unadenylylated PActa crystallographica. Section D, Structural biology · 2021Article
- The novel PProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Increasing the Ascomycin Yield by Relieving the Inhibition of Acetyl/Propionyl-CoA Carboxylase by the Signal Transduction Protein GlnB.Frontiers in microbiology · 2021Article
- Article
- NADThe Journal of biological chemistry · 2020Article
- Interaction of N-acetyl-l-glutamate kinase with the PII signal transducer in the non-photosynthetic alga Polytomella parva: Co-evolution towards a hetero-oligomeric enzyme.The FEBS journal · 2020Article
- Carbon/nitrogen homeostasis control in cyanobacteria.FEMS microbiology reviews · 2020Review
- Tuning the in vitro sensing and signaling properties of cyanobacterial PII protein by mutation of key residues.Scientific reports · 2019Article
- The Signal Transduction Protein PFrontiers in microbiology · 2019Article
- Dual positive and negative control of Chlamydomonas PII signal transduction protein expression by nitrate/nitrite and NO via the components of nitric oxide cycle.BMC plant biology · 2018Article
- A glutamine riboswitch is a key element for the regulation of glutamine synthetase in cyanobacteria.Nucleic acids research · 2018Article
- Biosensors-Based In Vivo Quantification of 2-Oxoglutarate in Cyanobacteria and Proteobacteria.Life (Basel, Switzerland) · 2018Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
P(II) proteins control key processes of nitrogen metabolism in bacteria, archaea, and plants in response to the central metabolites ATP, ADP, and 2-oxoglutarate (2-OG), signaling cellular energy and carbon and nitrogen abundance. This metabolic information is integrated by P(II) and transmitted to regulatory targets (key enzymes, transporters, and transcription factors), modulating their activity. In oxygenic phototrophs, the controlling enzyme of arginine synthesis, N-acetyl-glutamate kinase (NAGK), is a major P(II) target, whose activity responds to 2-OG via P(II). Here we show structures of the Synechococcus elongatus P(II) protein in complex with ATP, Mg(2+), and 2-OG, which clarify how 2-OG affects P(II)-NAGK interaction. P(II) trimers with all three sites fully occupied were obtained as well as structures with one or two 2-OG molecules per P(II) trimer. These structures identify the site of 2-OG located in the vicinity between the subunit clefts and the base of the T loop. The 2-OG is bound to a Mg(2+) ion, which is coordinated by three phosphates of ATP, and by ionic interactions with the highly conserved residues K58 and Q39 together with B- and T-loop backbone interactions. These interactions impose a unique T-loop conformation that affects the interactions with the P(II) target. Structures of P(II) trimers with one or two bound 2-OG molecules reveal the basis for anticooperative 2-OG binding and shed light on the intersubunit signaling mechanism by which P(II) senses effectors in a wide range of concentrations.
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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.