5KTE

Crystal structure of Deinococcus radiodurans MntH, an Nramp-family transition metal transporter

Summary for 5KTE

• Entry DOI: 10.2210/pdb5kte/pdb
• Descriptor: Divalent metal cation transporter MntH, Fab Heavy Chain, Fab Light Chain, ... (4 entities in total)
• Functional Keywords: divalent metal, transporter, nramp, leut fold, transport protein-immune system complex, transport protein/immune system
• Biological source: Deinococcus radiodurans; More
• Total number of polymer chains: 3
• Total formula weight: 91906.11

Authors

Bane, L.B.,Gaudet, R.,Weihofen, W.A.,Singharoy, A. (deposition date: 2016-07-11, release date: 2016-11-23, Last modification date: 2024-11-20)

Primary citation

Bozzi, A.T.,Bane, L.B.,Weihofen, W.A.,Singharoy, A.,Guillen, E.R.,Ploegh, H.L.,Schulten, K.,Gaudet, R.
Crystal Structure and Conformational Change Mechanism of a Bacterial Nramp-Family Divalent Metal Transporter.
Structure, 24:2102-2114, 2016

PubMed Abstract: 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 our cysteine accessibility scanning results onto this structure, we identified the metal-permeation pathway in the alternate outward-open conformation. We investigated the functional impact of two natural anemia-causing glycine-to-arginine mutations that impaired transition metal transport in both human Nramp2 and DraNramp. The TM4 G153R mutation perturbs the closing of the outward metal-permeation pathway and alters the selectivity of the conserved metal-binding site. In contrast, the TM1a G45R mutation prevents conformational change by sterically blocking the essential movement of that helix, thus locking the transporter in an inward-facing state.

PubMed: 27839948
DOI: 10.1016/j.str.2016.09.017

Experimental method

X-RAY DIFFRACTION (3.941 Å)