5KTE

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

5KTE の概要

• エントリーDOI: 10.2210/pdb5kte/pdb
• 分子名称: Divalent metal cation transporter MntH, Fab Heavy Chain, Fab Light Chain, ... (4 entities in total)
• 機能のキーワード: divalent metal, transporter, nramp, leut fold, transport protein-immune system complex, transport protein/immune system
• 由来する生物種: Deinococcus radiodurans; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 91906.11

構造登録者

Bane, L.B.,Gaudet, R.,Weihofen, W.A.,Singharoy, A. (登録日: 2016-07-11, 公開日: 2016-11-23, 最終更新日: 2024-11-20)

主引用文献

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

実験手法

X-RAY DIFFRACTION (3.941 Å)