7qji

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7qji FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qji OCA], [https://pdbe.org/7qji PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qji RCSB], [https://www.ebi.ac.uk/pdbsum/7qji PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qji ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

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(2+) and Mg(2+), 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(2+). The protein transports Mg(2+) and Mn(2+) but not Ca(2+) 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.

Structural and functional properties of a magnesium transporter of the SLC11/NRAMP family.,Ramanadane K, Straub MS, Dutzler R, Manatschal C Elife. 2022 Jan 10;11:e74589. doi: 10.7554/eLife.74589. PMID:35001872<ref>PMID:35001872</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

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