Structural and functional properties of a magnesium transporter of the SLC11/NRAMP family
| Autor: | Karthik Ramanadane, Monique S Straub, Raimund Dutzler, Cristina Manatschal |
|---|---|
| Přispěvatelé: | University of Zurich, Manatschal, Cristina |
| Rok vydání: | 2021 |
| Předmět: |
QH301-705.5
Stereochemistry Science Structural Biology and Molecular Biophysics Magnesium transporter x-ray crystallogrpahy 610 Medicine & health General Biochemistry Genetics and Molecular Biology Divalent Ion binding 1300 General Biochemistry Genetics and Molecular Biology 2400 General Immunology and Microbiology 10019 Department of Biochemistry Magnesium Biology (General) Cation Transport Proteins chemistry.chemical_classification General Immunology and Microbiology Bacteria Chemistry General Neuroscience 2800 General Neuroscience Transporter General Medicine isothermal titration calorimetry magnesium transport Solvation shell Cytoplasm Medicine cryo-EM 570 Life sciences biology Other Cotransporter Energy source transport assays Research Article |
| Zdroj: | eLife eLife, Vol 11 (2022) |
| DOI: | 10.1101/2021.10.17.464711 |
| Popis: | Members of the ubiquitous SLC11/NRAMP family catalyze the uptake of divalent transition metal ions into cells. They have evolved to efficiently select these trace elements from a large pool of Ca2+and Mg2+, which are both orders of magnitude more abundant, and to concentrate them in the cytoplasm aided by the cotransport of H+serving as energy source. In the present study, we have characterized a member of a distant clade of the family found in prokaryotes, termed NRMTs, that were proposed to function as transporters of Mg2+. The protein transports Mg2+and Mn2+but not Ca2+by a mechanism that is not coupled to H+. Structures determined by cryo-EM and X-ray crystallography revealed a generally similar protein architecture compared to classical NRAMPs, with a restructured ion binding site whose increased volume provides suitable interactions with ions that likely have retained much of their hydration shell. |
| Databáze: | OpenAIRE |
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