7QJJ
X-Ray Structure of a Mn2+ soak of EleNRMT in complex with two Nanobodies at 4.6A
Summary for 7QJJ
| Entry DOI | 10.2210/pdb7qjj/pdb |
| Related | 7QIA |
| EMDB information | 13985 |
| Descriptor | Divalent metal cation transporter, Elen-Nb1-Nb2, MANGANESE (II) ION, ... (4 entities in total) |
| Functional Keywords | slc11, nramp-related mg2+ transporter, nanobody complex, membrane protein |
| Biological source | Vicugna pacos More |
| Total number of polymer chains | 6 |
| Total formula weight | 146416.53 |
| Authors | Ramanadane, K.,Straub, M.S.,Dutzler, R.,Manatschal, C. (deposition date: 2021-12-16, release date: 2022-02-02, Last modification date: 2024-10-16) |
| Primary citation | Ramanadane, K.,Straub, M.S.,Dutzler, R.,Manatschal, C. Structural and functional properties of a magnesium transporter of the SLC11/NRAMP family. Elife, 11:-, 2022 Cited by 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 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. PubMed: 35001872DOI: 10.7554/eLife.74589 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (4.6 Å) |
Structure validation
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