ArticleProceedings of the National Academy of Sciences of the United States of America2005
Crystal structure of the archaeal ammonium transporter Amt-1 from Archaeoglobus fulgidus.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 110 papers.
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110 citing papers in PubMed, 216 citations in OpenAlex.
- Ammonia oxidizers offset acidification stress via adaptive substrate affinity in aquatic ecosystems.Nature communications · 2026Article
- The RNF/NQR redox pumps: a versatile system for energy transduction in bacteria and archaea.Applied microbiology and biotechnology · 2025Review
- Extensive paralogism in the environmental pangenome: a key factor in the ecological success of natural SAR11 populations.Microbiome · 2025Article
- Ammonium Transporter 1 (Current issues in molecular biology · 2025Article
- Adaptive traits ofmBio · 2024Article
- How sensor Amt-like proteins integrate ammonium signals.Science advances · 2024Article
- Biological ammonium transporters from the Amt/Mep/Rh superfamily: mechanism, energetics, and technical limitations.Bioscience reports · 2024Review
- Conformational coupling of redox-driven NaNature structural & molecular biology · 2023Article
- Nitrification and beyond: metabolic versatility of ammonia oxidising archaea.The ISME journal · 2023Review
- Prokaryotic ammonium transporters: what has three decades of research revealed?Microbiology (Reading, England) · 2023Article
- Expression and Functional Analysis ofAnimals : an open access journal from MDPI · 2023Article
- Identification and functional characterization of the sugarcane (Frontiers in plant science · 2023Article
- The Exploring Functional Role of Ammonium Transporters ofInternational journal of molecular sciences · 2022Article
- Exaggerated trans-membrane charge of ammonium transporters in nutrient-poor marine environments.Open biology · 2022Article
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- High-pressure crystallography shows noble gas intervention into protein-lipid interaction and suggests a model for anaesthetic action.Communications biology · 2022Article
- Plant DNA methylation is sensitive to parent seed N content and influences the growth of rice.BMC plant biology · 2021Article
- Article
- A twin histidine motif is the core structure for high-affinity substrate selection in plant ammonium transporters.The Journal of biological chemistry · 2020Article
- Yeast filamentation signaling is connected to a specific substrate translocation mechanism of the Mep2 transceptor.PLoS genetics · 2020Article
50 more citing papers are in PubMed but not listed here.
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4 authors at 1 institution in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
Ammonium transporters (Amts) are integral membrane proteins found in all kingdoms of life that fulfill an essential function in the uptake of reduced nitrogen for biosynthetic purposes. Amt-1 is one of three Amts encoded in the genome of the hyperthermophilic archaeon Archaeoglobus fulgidus. The crystal structure of Amt-1 shows a compact trimer with 11 transmembrane helices per monomer and a central channel for substrate conduction in each monomer, similar to the known crystal structure of AmtB from Escherichia coli. Xenon derivatization has been used to identify apolar regions of Amt-1, emphasizing not only the hydrophobicity of the substrate channel but also the unexpected presence of extensive internal cavities that should be detrimental for protein stability. The substrates ammonium and methylammonium have been used for cocrystallization experiments with Amt-1, but the identification of binding sites that are distinct from water positions is not unambiguous. The well ordered cytoplasmic C terminus of the protein in the Amt-1 structure has allowed for the construction of a docking model between Amt-1 and a homology model for its physiological interaction partner, the P(II) protein GlnB-1. In this model, GlnB-1 binds tightly to the cytoplasmic face of the transporter, effectively blocking conduction through the three individual substrate channels.
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