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7QJI

X-Ray Structure of apo-EleNRMT in complex with two Nanobodies at 4.1A

Summary for 7QJI
Entry DOI10.2210/pdb7qji/pdb
Related7QIA
EMDB information13985
DescriptorDivalent metal cation transporter, Elen-Nanobody-complex (3 entities in total)
Functional Keywordsslc11, nramp-related mg2+ transporter, nanobody complex, membrane protein
Biological sourceVicugna pacos
More
Total number of polymer chains6
Total formula weight146306.66
Authors
Ramanadane, K.,Straub, M.S.,Dutzler, R.,Manatschal, C. (deposition date: 2021-12-16, release date: 2022-02-02, Last modification date: 2024-10-23)
Primary citationRamanadane, 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: 35001872
DOI: 10.7554/eLife.74589
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (4.1 Å)
Structure validation

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