Structural and functional properties of a magnesium transporter of the SLC11/NRAMP family
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 a...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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eLife Sciences Publications Ltd
2022-01-01
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| Series: | eLife |
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| Online Access: | https://elifesciences.org/articles/74589 |
| _version_ | 1797998457460359168 |
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| author | Karthik Ramanadane Monique S Straub Raimund Dutzler Cristina Manatschal |
| author_facet | Karthik Ramanadane Monique S Straub Raimund Dutzler Cristina Manatschal |
| author_sort | Karthik Ramanadane |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-04-11T10:49:02Z |
| format | Article |
| id | doaj.art-9f29a7d4cef94419b4caf7ae3d8f0f34 |
| institution | Directory Open Access Journal |
| issn | 2050-084X |
| language | English |
| last_indexed | 2024-04-11T10:49:02Z |
| publishDate | 2022-01-01 |
| publisher | eLife Sciences Publications Ltd |
| record_format | Article |
| series | eLife |
| spelling | doaj.art-9f29a7d4cef94419b4caf7ae3d8f0f342022-12-22T04:28:58ZengeLife Sciences Publications LtdeLife2050-084X2022-01-011110.7554/eLife.74589Structural and functional properties of a magnesium transporter of the SLC11/NRAMP familyKarthik Ramanadane0https://orcid.org/0000-0001-7188-0250Monique S Straub1https://orcid.org/0000-0002-7721-5048Raimund Dutzler2https://orcid.org/0000-0002-2193-6129Cristina Manatschal3https://orcid.org/0000-0002-4907-7303Department of Biochemistry, University of Zurich, Zurich, SwitzerlandDepartment of Biochemistry, University of Zurich, Zurich, SwitzerlandDepartment of Biochemistry, University of Zurich, Zurich, SwitzerlandDepartment of Biochemistry, University of Zurich, Zurich, SwitzerlandMembers 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.https://elifesciences.org/articles/74589magnesium transportcryo-EMx-ray crystallogrpahytransport assaysisothermal titration calorimetry |
| spellingShingle | Karthik Ramanadane Monique S Straub Raimund Dutzler Cristina Manatschal Structural and functional properties of a magnesium transporter of the SLC11/NRAMP family eLife magnesium transport cryo-EM x-ray crystallogrpahy transport assays isothermal titration calorimetry |
| title | Structural and functional properties of a magnesium transporter of the SLC11/NRAMP family |
| title_full | Structural and functional properties of a magnesium transporter of the SLC11/NRAMP family |
| title_fullStr | Structural and functional properties of a magnesium transporter of the SLC11/NRAMP family |
| title_full_unstemmed | Structural and functional properties of a magnesium transporter of the SLC11/NRAMP family |
| title_short | Structural and functional properties of a magnesium transporter of the SLC11/NRAMP family |
| title_sort | structural and functional properties of a magnesium transporter of the slc11 nramp family |
| topic | magnesium transport cryo-EM x-ray crystallogrpahy transport assays isothermal titration calorimetry |
| url | https://elifesciences.org/articles/74589 |
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