- EMDB-50237: Human NRAMP1 (SLC11A1) in complex with manganese, towards the inw... -
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基本情報
登録情報
データベース: EMDB / ID: EMD-50237
タイトル
Human NRAMP1 (SLC11A1) in complex with manganese, towards the inward-open state
マップデータ
試料
複合体: Complex of NRAMP1 with manganese
タンパク質・ペプチド: Natural resistance-associated macrophage protein 1
リガンド: MANGANESE (II) ION
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
機能・相同性
機能・相同性情報
metal cation:proton antiporter activity / transition metal ion transmembrane transporter activity / nitrite transport / L-arginine transmembrane transport / cellular detoxification of cadmium ion / MHC class II biosynthetic process / cadmium ion transmembrane transport / Metal ion SLC transporters / Ion influx/efflux at host-pathogen interface / positive regulation of dendritic cell antigen processing and presentation ...metal cation:proton antiporter activity / transition metal ion transmembrane transporter activity / nitrite transport / L-arginine transmembrane transport / cellular detoxification of cadmium ion / MHC class II biosynthetic process / cadmium ion transmembrane transport / Metal ion SLC transporters / Ion influx/efflux at host-pathogen interface / positive regulation of dendritic cell antigen processing and presentation / manganese ion transport / cadmium ion transmembrane transporter activity / manganese ion transmembrane transporter activity / positive regulation of T-helper 1 type immune response / iron ion transmembrane transporter activity / metal ion transport / iron ion transmembrane transport / antigen processing and presentation of peptide antigen / respiratory burst / macrophage activation / ROS and RNS production in phagocytes / antimicrobial humoral response / vacuolar acidification / mRNA stabilization / negative regulation of cytokine production / defense response to protozoan / tertiary granule membrane / T cell proliferation involved in immune response / ficolin-1-rich granule membrane / response to type II interferon / phagocytosis / positive regulation of phagocytosis / cell redox homeostasis / positive regulation of cytokine production / establishment of localization in cell / response to bacterium / wound healing / multicellular organismal-level iron ion homeostasis / positive regulation of type II interferon production / phagocytic vesicle membrane / late endosome membrane / late endosome / iron ion transport / defense response to Gram-negative bacterium / response to lipopolysaccharide / intracellular iron ion homeostasis / lysosome / endosome membrane / defense response to bacterium / inflammatory response / lysosomal membrane / Neutrophil degranulation / positive regulation of gene expression / protein homodimerization activity / positive regulation of transcription by RNA polymerase II / plasma membrane 類似検索 - 分子機能
NRAMP family / Natural resistance-associated macrophage protein-like 類似検索 - ドメイン・相同性
Natural resistance-associated macrophage protein 1 類似検索 - 構成要素
ジャーナル: Nat Commun / 年: 2025 タイトル: Structural basis for metal ion transport by the human SLC11 proteins DMT1 and NRAMP1. 著者: Márton Liziczai / Ariane Fuchs / Cristina Manatschal / Raimund Dutzler / 要旨: 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 ...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.