ArticleStructure (London, England : 1993)2016
Crystal Structure and Conformational Change Mechanism of a Bacterial Nramp-Family Divalent Metal Transporter.
Article in Structure (London, England : 1993), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 70 citations in OpenAlex.
- The SLC-ome of membrane transport: from molecular discovery to physiology and clinical applications.Physiological reviews · 2026Review
- Genome-wide identification of NRAMP gene family in Brassica U's triangle species and its response to Cadmium stress in B. napus.BMC plant biology · 2026Article
- An N-terminal amphipathic helix governs activity and conformational dynamics of Nramp metal transporters.bioRxiv : the preprint server for biology · 2026Article
- Fluorescence-Based Ion Transport Assays Using Proteoliposomes.Bio-protocol · 2026Article
- Structural and functional basis of proton-independent transition metal import by a canonical bacterial Nramp transporter.bioRxiv : the preprint server for biology · 2026Article
- Calculation of minimum energy pathways in transport proteins.Communications chemistry · 2025Article
- Identification of a divalent metal transporter required for cellular iron metabolism in malaria parasites.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- In vitro reconstitution of transition metal transporters.The Journal of biological chemistry · 2024Review
- Identification of a divalent metal transporter required for cellular iron metabolism in malaria parasites.bioRxiv : the preprint server for biology · 2024Article
- Identification of novel single nucleotide variants in the drug resistance mechanism of Mycobacterium tuberculosis isolates by whole-genome analysis.BMC genomics · 2024Article
- Iron transport pathways in the human malaria parasiteFrontiers in cellular and infection microbiology · 2024Article
- Engineering rice Nramp5 modifies cadmium and manganese uptake selectivity using yeast assay system.Frontiers in plant science · 2024Article
- Membrane Transporters Involved in Iron Trafficking: Physiological and Pathological Aspects.Biomolecules · 2023Review
- Microbe-driven elemental cycling enables microbial adaptation to deep-sea ferromanganese nodule sediment fields.Microbiome · 2023Article
- The role of TMS 12 in the staphylococcal multidrug efflux protein QacA.The Journal of antimicrobial chemotherapy · 2023Article
- High-resolution structures with bound MneLife · 2023Article
- Structural insights into the elevator-type transport mechanism of a bacterial ZIP metal transporter.Nature communications · 2023Article
- A general protocol for the expression and purification of the intact transmembrane transporter FeoB.Biochimica et biophysica acta. Biomembranes · 2022Article
- The two-domain elevator-type mechanism of zinc-transporting ZIP proteins.Science advances · 2022Article
- Structural and functional properties of a magnesium transporter of the SLC11/NRAMP family.eLife · 2022Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
The widely conserved natural resistance-associated macrophage protein (Nramp) family of divalent metal transporters enables manganese import in bacteria and dietary iron uptake in mammals. We determined the crystal structure of the Deinococcus radiodurans Nramp homolog (DraNramp) in an inward-facing apo state, including the complete transmembrane (TM) segment 1a (absent from a previous Nramp structure). Mapping our cysteine accessibility scanning results onto this structure, we identified the metal-permeation pathway in the alternate outward-open conformation. We investigated the functional impact of two natural anemia-causing glycine-to-arginine mutations that impaired transition metal transport in both human Nramp2 and DraNramp. The TM4 G153R mutation perturbs the closing of the outward metal-permeation pathway and alters the selectivity of the conserved metal-binding site. In contrast, the TM1a G45R mutation prevents conformational change by sterically blocking the essential movement of that helix, thus locking the transporter in an inward-facing state.
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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.