7QIA

Structure of apo-EleNRMT in complex with two nanobodies at 3.5A

7QIA の概要

• エントリーDOI: 10.2210/pdb7qia/pdb
• EMDBエントリー: 13985
• 分子名称: Divalent metal cation transporter, Nanobody 1, Nanobody 2, ... (4 entities in total)
• 機能のキーワード: slc11, magnesium, leut fold, membrane protein
• 由来する生物種: Eggerthella lenta; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 73742.93

構造登録者

Ramanadane, K.,Straub, M.S.,Dutzler, R.,Manatschal, C. (登録日: 2021-12-14, 公開日: 2021-12-29, 最終更新日: 2024-10-23)

主引用文献

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

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

実験手法

ELECTRON MICROSCOPY (3.5 Å)