Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Transmembrane helix 6b links proton and metal release pathways and drives conformational change in an Nramp-family transition metal transporter.

The Journal of biological chemistry - 31 Jan 2020

Bozzi Aaron T, McCabe Anne L, Barnett Benjamin C, Gaudet Rachelle

Abstract excerpt

The natural resistance-associated macrophage protein (Nramp) family encompasses transition metal and proton cotransporters that are present in many organisms from bacteria to humans. Recent structures of Deinococcus radiodurans Nramp (DraNramp) in multiple conformations revealed the intramolecular rearrangements required for alternating access of the metal-binding site to the external or cytosolic environment....

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cobalt
Share to Deinococcus

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Histidine

Share to Hydrophobic and Hydrophilic Interactions

Share to Ion Transport

Share to Manganese

Share to Metals

Share to Protons

Source

Open in PubMed Open full text

Identifiers

PMID: 31882536
DOI: 10.1074/jbc.RA119.011336
PMCID: PMC6996879

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Transmembrane helix 6b links proton and metal release pathways and drives conformational change in an Nramp-family transition metal transporter.PMID 31882536Read ↗

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

Recent progress in structure-function analyses of Nramp proton-dependent metal-ion transporters.Semantic proximity Read ↗

Structural and mechanistic basis of proton-coupled metal ion transport in the SLC11/NRAMP family.Semantic proximity Read ↗

Conformational rearrangements in the N-domain of Escherichia coli FepA during ferric enterobactin transport.Semantic proximity Read ↗

Relocation of active site carboxylates in major facilitator superfamily multidrug transporter LmrP reveals plasticity in proton interactions.Semantic proximity Read ↗

Natural resistance to intracellular infections: natural resistance-associated macrophage protein 1 (Nramp1) functions as a pH-dependent manganese transporter at the phagosomal membrane.Semantic proximity Read ↗

Differential Roles of Extracellular Histidine Residues of GPR68 for Proton-Sensing and Allosteric Modulation by Divalent Metal Ions.Semantic proximity Read ↗

Mechanistic insights into staphylopine-mediated metal acquisitionSemantic proximity Read ↗

The metal binding site composition of the cation diffusion facilitator protein MamM cytoplasmic domain impacts its metal responsivity.Semantic proximity Read ↗

Prokaryotic ammonium transporters: what has three decades of research revealed?Semantic proximity Read ↗

Basic residues R260 and K357 affect the conformational dynamics of the major facilitator superfamily multidrug transporter LmrP.Semantic proximity Read ↗

DR1440 is a potential iron efflux protein involved in maintenance of iron homeostasis and resistance of Deinococcus radiodurans to oxidative stress.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.