ArticleProceedings of the National Academy of Sciences of the United States of America2007
The crystal structure of the Escherichia coli AmtB-GlnK complex reveals how GlnK regulates the ammonia channel.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 97 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
97 citing papers in PubMed, 184 citations in OpenAlex.
- Functional and structural insights into cyanobacterial COThe Plant journal : for cell and molecular biology · 2026Review
- Glnk Mediates Carbapenem Resistance Through the NtrB/NtrC-OprD Regulatory Pathway inPathogens (Basel, Switzerland) · 2026Article
- Kinetic plasticity of nitrite-oxidizing bacteria containing cytoplasmic nitrite oxidoreductase.The ISME journal · 2026Article
- Activation of a Secondary-Messenger Receptor via Allosteric Modulation of a Dynamic Conformational Ensemble.Angewandte Chemie (International ed. in English) · 2025Article
- Ammonium Transporter 1 (Current issues in molecular biology · 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
- The PII protein interacts with the Amt ammonium transport and modulates nitrate/nitrite assimilation in mycobacteria.Frontiers in microbiology · 2024Article
- M. mazei glutamine synthetase and glutamine synthetase-GlnK1 structures reveal enzyme regulation by oligomer modulation.Nature communications · 2023Article
- Flipping the switch: dynamic modulation of membrane transporter activity in bacteria.Microbiology (Reading, England) · 2023Review
- Prokaryotic ammonium transporters: what has three decades of research revealed?Microbiology (Reading, England) · 2023Article
- Isolation and Genomics ofMicrobiology spectrum · 2023Article
- Roles of second messengers in the regulation of cyanobacterial physiology: the carbon-concentrating mechanism and beyond.microLife · 2023Review
- Variable-Temperature Native Mass Spectrometry for Studies of Protein Folding, Stabilities, Assembly, and Molecular Interactions.Annual review of biophysics · 2022Review
- Metabolic Diversity and Aero-Tolerance in Anammox Bacteria from Geochemically Distinct Aquifers.mSystems · 2022Article
- Production of l-glutamate family amino acids inSynthetic and systems biotechnology · 2021Review
- The Oxoglutarate Binding Site and Regulatory Mechanism Are Conserved in Ammonium Transporter Inhibitors GlnKs fromInternational journal of molecular sciences · 2021Article
- Structures of cyanobacterial bicarbonate transporter SbtA and its complex with PII-like SbtB.Cell discovery · 2021Article
- Molecular mechanism underlying transport and allosteric inhibition of bicarbonate transporter SbtA.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Potential virus-mediated nitrogen cycling in oxygen-depleted oceanic waters.The ISME journal · 2021Article
- PII Signal Transduction Protein GlnK Alleviates Feedback Inhibition ofApplied and environmental microbiology · 2020Article
37 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
Amt proteins are ubiquitous channels for the conduction of ammonia in archaea, eubacteria, fungi, and plants. In Escherichia coli, previous studies have indicated that binding of the PII signal transduction protein GlnK to the ammonia channel AmtB regulates the channel thereby controlling ammonium influx in response to the intracellular nitrogen status. Here, we describe the crystal structure of the complex between AmtB and GlnK at a resolution of 2.5 A. This structure of PII in a complex with one of its targets reveals physiologically relevant conformations of both AmtB and GlnK. GlnK interacts with AmtB almost exclusively via a long surface loop containing Y51 (T-loop), the tip of which inserts deeply into the cytoplasmic pore exit, blocking ammonia conduction. Y51 of GlnK is also buried in the pore exit, explaining why uridylylation of this residue prevents complex formation.
Indexed as
Identifiers
What OpenQuestion holds
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.