ArticleThe EMBO journal2007
Structure of GlnK1 with bound effectors indicates regulatory mechanism for ammonia uptake.
Article in The EMBO journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 64 citations in OpenAlex.
- Article
- The Oxoglutarate Binding Site and Regulatory Mechanism Are Conserved in Ammonium Transporter Inhibitors GlnKs fromInternational journal of molecular sciences · 2021Article
- Crystal structures of adenylylated and unadenylylated PActa crystallographica. Section D, Structural biology · 2021Article
- An HIV Vaccine Targeting the V2 Region of the HIV Envelope Induces a Highly Durable Polyfunctional Fc-Mediated Antibody Response in Rhesus Macaques.Journal of virology · 2020Article
- Multimeric Epitope-Scaffold HIV Vaccines Target V1V2 and Differentially Tune Polyfunctional Antibody Responses.Cell reports · 2019Article
- Rationally Designed Vaccines Targeting the V2 Region of HIV-1 gp120 Induce a Focused, Cross-Clade-Reactive, Biologically Functional Antibody Response.Journal of virology · 2016Article
- A PII-Like Protein Regulated by Bicarbonate: Structural and Biochemical Studies of the Carboxysome-Associated CPII Protein.Journal of molecular biology · 2016Article
- Identification, characterization, and structure analysis of the cyclic di-AMP-binding PII-like signal transduction protein DarA.The Journal of biological chemistry · 2015Article
- Complex structure and biochemical characterization of the Staphylococcus aureus cyclic diadenylate monophosphate (c-di-AMP)-binding protein PstA, the founding member of a new signal transduction protein family.The Journal of biological chemistry · 2015Article
- Structural basis and target-specific modulation of ADP sensing by the Synechococcus elongatus PII signaling protein.The Journal of biological chemistry · 2014Article
- P(II) signal transduction proteins are ATPases whose activity is regulated by 2-oxoglutarate.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Imaging energy status in live cells with a fluorescent biosensor of the intracellular ATP-to-ADP ratio.Nature communications · 2013Article
- Overcoming fluctuation and leakage problems in the quantification of intracellular 2-oxoglutarate levels in Escherichia coli.Applied and environmental microbiology · 2011Article
- Genetically encodable fluorescent biosensors for tracking signaling dynamics in living cells.Chemical reviews · 2011Review
- Structure of GlnK1, a signalling protein from Archaeoglobus fulgidus.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011Article
- Mechanism of disruption of the Amt-GlnK complex by P(II)-mediated sensing of 2-oxoglutarate.PloS one · 2011Article
- Mechanism of 2-oxoglutarate signaling by the Synechococcus elongatus PII signal transduction protein.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Structural underpinnings of nitrogen regulation by the prototypical nitrogen-responsive transcriptional factor NrpR.Structure (London, England : 1993) · 2010Article
- Control of AmtB-GlnK complex formation by intracellular levels of ATP, ADP, and 2-oxoglutarate.The Journal of biological chemistry · 2010Article
- Structural basis for the regulation of NtcA-dependent transcription by proteins PipX and PII.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A binary complex of the ammonia channel Amt1 from Methanococcus jannaschii and its cognate P(II) signalling protein GlnK1 has been produced and characterized. Complex formation is prevented specifically by the effector molecules Mg-ATP and 2-ketoglutarate. Single-particle electron microscopy of the complex shows that GlnK1 binds on the cytoplasmic side of Amt1. Three high-resolution X-ray structures of GlnK1 indicate that the functionally important T-loop has an extended, flexible conformation in the absence of Mg-ATP, but assumes a compact, tightly folded conformation upon Mg-ATP binding, which in turn creates a 2-ketoglutarate-binding site. We propose a regulatory mechanism by which nitrogen uptake is controlled by the binding of both effector molecules to GlnK1. At normal effector levels, a 2-ketoglutarate molecule binding at the apex of the compact T-loop would prevent complex formation, ensuring uninhibited ammonia uptake. At low levels of Mg-ATP, the extended loops would seal the ammonia channels in the complex. Binding of both effector molecules to P(II) signalling proteins may thus represent an effective feedback mechanism for regulating ammonium uptake through the membrane.
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