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TitleStructural basis for metal ion transport by the human SLC11 proteins DMT1 and NRAMP1.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 761, Year 2025
Publish dateJan 17, 2025
AuthorsMárton Liziczai / Ariane Fuchs / Cristina Manatschal / Raimund Dutzler /
PubMed AbstractIron 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.
External linksNat Commun / PubMed:39824808 / PubMed Central
MethodsEM (single particle)
Resolution3.6 - 3.9 Å
Structure data

50235

9f6n

EMDB-50235, PDB-9f6n:
Human divalent metal transporter 1 (DMT1/SLC11A2) in complex with manganese, in an occluded state
Method: EM (single particle) / Resolution: 3.6 Å

50236

9f6o

EMDB-50236, PDB-9f6o:
Human divalent metal transporter 1 (DMT1/SLC11A2) in complex with sybody 1, in an occluded state
Method: EM (single particle) / Resolution: 3.9 Å

50237

9f6p

EMDB-50237, PDB-9f6p:
Human NRAMP1 (SLC11A1) in complex with manganese, towards the inward-open state
Method: EM (single particle) / Resolution: 3.7 Å

50238

9f6q

EMDB-50238, PDB-9f6q:
Human NRAMP1 (SLC11A1) in an occluded state
Method: EM (single particle) / Resolution: 3.9 Å

Chemicals

ChemComp-MN:
Unknown entry

Source
  • homo sapiens (human)
  • synthetic construct (others)
KeywordsTRANSPORT PROTEIN / 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 / NRAMP

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