8ONT

Structure of Setaria italica NRAT in complex with a nanobody

8ONT の概要

• エントリーDOI: 10.2210/pdb8ont/pdb
• EMDBエントリー: 17000
• 分子名称: NRAMP related aluminium transporter, Nanobody1, DIUNDECYL PHOSPHATIDYL CHOLINE, ... (4 entities in total)
• 機能のキーワード: nrat, nramp, slc11, metal uptake, aluminium transporter, transport protein
• 由来する生物種: Setaria italica (foxtail millet); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 73841.61

構造登録者

Ramanadane, K.,Liziczai, M.,Markovic, D.,Straub, M.S.,Rosalen, G.T.,Udovcic, A.,Dutzler, R.,Manatschal, C. (登録日: 2023-04-03, 公開日: 2023-04-12, 最終更新日: 2025-07-09)

主引用文献

Ramanadane, K.,Liziczai, M.,Markovic, D.,Straub, M.S.,Rosalen, G.T.,Udovcic, A.,Dutzler, R.,Manatschal, C.
Structural and functional properties of a plant NRAMP-related aluminum transporter.
Elife, 12:-, 2023

PubMed Abstract: The transport of transition metal ions by members of the SLC11/NRAMP family constitutes a ubiquitous mechanism for the uptake of Fe and Mn across all kingdoms of life. Despite the strong conservation of the family, two of its branches have evolved a distinct substrate preference with one mediating Mg uptake in prokaryotes and another the transport of Al into plant cells. Our previous work on the SLC11 transporter from revealed the basis for its Mg selectivity (Ramanadane et al., 2022). Here, we have addressed the structural and functional properties of a putative Al transporter from . We show that the protein transports diverse divalent metal ions and binds the trivalent ions Al and Ga, which are both presumable substrates. Its cryo-electron microscopy (cryo-EM) structure displays an occluded conformation that is closer to an inward- than an outward-facing state, with a binding site that is remodeled to accommodate the increased charge density of its transported substrate.

PubMed: 37074929
DOI: 10.7554/eLife.85641

実験手法

ELECTRON MICROSCOPY (3.66 Å)