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Article

Crystal Structure and Conformational Change Mechanism of a Bacterial Nramp-Family Divalent Metal Transporter.

Structure (London, England : 1993) - 6 Dec 2016

Bozzi Aaron T, Bane Lukas B, Weihofen Wilhelm A, Singharoy Abhishek, Guillen Eduardo R, Ploegh Hidde L, Schulten Klaus, Gaudet Rachelle

Abstract excerpt

The widely conserved natural resistance-associated macrophage protein (Nramp) family of divalent metal transporters enables manganese import in bacteria and dietary iron uptake in mammals. We determined the crystal structure of the Deinococcus radiodurans Nramp homolog (DraNramp) in an inward-facing apo state, including the complete transmembrane (TM) segment 1a (absent from a previous Nramp structure). Mapping...

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Identifiers

PMID: 27839948
DOI: 10.1016/j.str.2016.09.017
PMCID: PMC5143219

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

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