7QIA
Structure of apo-EleNRMT in complex with two nanobodies at 3.5A
Summary for 7QIA
| Entry DOI | 10.2210/pdb7qia/pdb |
| EMDB information | 13985 |
| Descriptor | Divalent metal cation transporter, Nanobody 1, Nanobody 2, ... (4 entities in total) |
| Functional Keywords | slc11, magnesium, leut fold, membrane protein |
| Biological source | Eggerthella lenta More |
| Total number of polymer chains | 3 |
| Total formula weight | 73742.93 |
| Authors | Ramanadane, K.,Straub, M.S.,Dutzler, R.,Manatschal, C. (deposition date: 2021-12-14, release date: 2021-12-29, Last modification date: 2024-10-23) |
| 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 | ELECTRON MICROSCOPY (3.5 Å) |
Structure validation
Download full validation report
