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-Structure paper
Title | Structural and functional properties of a magnesium transporter of the SLC11/NRAMP family. |
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Journal, issue, pages | Elife, Vol. 11, Year 2022 |
Publish date | Jan 10, 2022 |
Authors | Karthik Ramanadane / Monique S Straub / Raimund Dutzler / Cristina Manatschal / |
PubMed Abstract | 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 Ca and ...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 Ca and Mg, 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 Mg. The protein transports Mg and Mn but not Ca 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. |
External links | Elife / PubMed:35001872 / PubMed Central |
Methods | EM (single particle) / X-ray diffraction |
Resolution | 3.5 - 4.6 Å |
Structure data | EMDB-13985: Cryo-EM map of apo-EleNRMT in complex with two nanobodies at 3.5A EMDB-13987: Cryo-EM map of magnesium-bound EleNRMT in complex with two nanobodies at 4.1A PDB-7qji: PDB-7qjj: |
Chemicals | ChemComp-HOH: ChemComp-MG: ChemComp-MN: |
Source |
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Keywords | MEMBRANE PROTEIN / SLC11 / Magnesium / LeuT fold / NRAMP-related Mg2+ transporter / Nanobody complex |