9F6Q

Human NRAMP1 (SLC11A1) in an occluded state

9F6Q の概要

• エントリーDOI: 10.2210/pdb9f6q/pdb
• EMDBエントリー: 50238
• 分子名称: Natural resistance-associated macrophage protein 1 (1 entity in total)
• 機能のキーワード: iron transport, manganese transport, transition metal transport, divalent metal transport, metal transport, transporter, membrane protein, slc, iron uptake, iron homeostasis, leut fold, small membrane protein, transport protein, nramp
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 67100.83

構造登録者

Liziczai, M.,Dutzler, R. (登録日: 2024-05-02, 公開日: 2024-11-27, 最終更新日: 2025-07-02)

主引用文献

Liziczai, M.,Fuchs, A.,Manatschal, C.,Dutzler, R.
Structural basis for metal ion transport by the human SLC11 proteins DMT1 and NRAMP1.
Nat Commun, 16:761-761, 2025

PubMed Abstract: Iron and manganese are essential nutrients whose transport across membranes is catalyzed by members of the SLC11 family. In humans, this protein family contains two paralogs, the ubiquitously expressed DMT1, which is involved in the uptake and distribution of Fe and Mn, and NRAMP1, which participates in the resistance against infections and nutrient recycling. Despite previous studies contributing to our mechanistic understanding of the family, the structures of human SLC11 proteins and their relationship to functional properties have remained elusive. Here we describe the cryo-electron microscopy structures of DMT1 and NRAMP1 and relate them to their functional properties. We show that both proteins catalyze selective metal ion transport coupled to the symport of H, but additionally also mediate uncoupled H flux. Their structures, while sharing general properties with known prokaryotic homologs, display distinct features that lead to stronger transition metal ion selectivity.

PubMed: 39824808
DOI: 10.1038/s41467-024-54705-0

実験手法

ELECTRON MICROSCOPY (3.9 Å)