ArticleProceedings of the National Academy of Sciences of the United States of America2007
The 1.3-A resolution structure of Nitrosomonas europaea Rh50 and mechanistic implications for NH3 transport by Rhesus family proteins.
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 64 papers.
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64 citing papers in PubMed, 124 citations in OpenAlex.
- The SLC-ome of membrane transport: from molecular discovery to physiology and clinical applications.Physiological reviews · 2026Review
- Hypoxia and acidification antagonistically suppress nitrification but enhance its NScience advances · 2026Article
- Protein Structures of Urea Transporters.Sub-cellular biochemistry · 2025Review
- How sensor Amt-like proteins integrate ammonium signals.Science advances · 2024Article
- Dating Ammonia-Oxidizing Bacteria with Abundant Eukaryotic Fossils.Molecular biology and evolution · 2024Article
- Biological ammonium transporters from the Amt/Mep/Rh superfamily: mechanism, energetics, and technical limitations.Bioscience reports · 2024Review
- Molecular dynamics of the human RhD and RhAG blood group proteins.Frontiers in chemistry · 2024Article
- Nitrification and beyond: metabolic versatility of ammonia oxidising archaea.The ISME journal · 2023Review
- Distinct Nitrification Rates and Nitrifiers in Needleleaf and Evergreen Broadleaf Forest Soils.Microbial ecology · 2023Article
- Prokaryotic ammonium transporters: what has three decades of research revealed?Microbiology (Reading, England) · 2023Article
- Nitrite accumulation and anammox bacterial niche partitioning in Arctic Mid-Ocean Ridge sediments.ISME communications · 2023Article
- Two closely related ureotelic fish species of the genus Alcolapia express different levels of ammonium transporters in gills.Biology open · 2022Article
- Exaggerated trans-membrane charge of ammonium transporters in nutrient-poor marine environments.Open biology · 2022Article
- Article
- Association of Blood Group Antigen CD59 with Disease.Transfusion medicine and hemotherapy : offizielles Organ der Deutschen Gesellschaft fur Transfusionsmedizin und Immunhamatologie · 2022Review
- Production and Excretion of Polyamines To Tolerate High Ammonia, a Case Study on Soil Ammonia-Oxidizing Archaeon "mSystems · 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
- Nutrient Limitation Causes Differential Expression of Transport- and Metabolism Genes in the Compartmentalized Anammox BacteriumFrontiers in microbiology · 2020Article
4 more citing papers are in PubMed but not listed here.
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Authors and funding
8 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Rhesus (Rh) proteins are a family of integral membrane proteins found throughout the animal kingdom that also occur in a number of lower eukaryotes. The significance of Rh proteins derives from their presence in the human red blood cell membrane, where they constitute the second most important group of antigens used in transfusion medicine after the ABO group. Rh proteins are related to the ammonium transport (Amt) protein family and there is considerable evidence that, like Amt proteins, they function as ammonia channels. We have now solved the structure of a rare bacterial homologue (from Nitrosomonas europaea) of human Rh50 proteins at a resolution of 1.3 A. The protein is a trimer, and analysis of its subunit interface strongly argues that all Rh proteins are likely to be homotrimers and that the human erythrocyte proteins RhAG and RhCE/D are unlikely to form heterooligomers as previously proposed. When compared with structures of bacterial Amt proteins, NeRh50 shows several distinctive features of the substrate conduction pathway that support the concept that Rh proteins have much lower ammonium affinities than Amt proteins and might potentially function bidirectionally.
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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.