6D9W

Crystal structure of Deinococcus radiodurans MntH, an Nramp-family transition metal transporter, in the inward-open apo state

6D9W の概要

• エントリーDOI: 10.2210/pdb6d9w/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: transition metal, proton, secondary transporter, leut-fold, transport protein
• 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

Gaudet, R.,Bane, L.B.,Weihofen, W.A.,Singharoy, A.,Zimanyi, C.M.,Bozzi, A.T. (登録日: 2018-04-30, 公開日: 2019-02-13, 最終更新日: 2024-11-20)

主引用文献

Bozzi, A.T.,Zimanyi, C.M.,Nicoludis, J.M.,Lee, B.K.,Zhang, C.H.,Gaudet, R.
Structures in multiple conformations reveal distinct transition metal and proton pathways in an Nramp transporter.
Elife, 8:-, 2019

PubMed Abstract: Nramp family transporters-expressed in organisms from bacteria to humans-enable uptake of essential divalent transition metals via an alternating-access mechanism that also involves proton transport. We present high-resolution structures of (Dra)Nramp in multiple conformations to provide a thorough description of the Nramp transport cycle by identifying the key intramolecular rearrangements and changes to the metal coordination sphere. Strikingly, while metal transport requires cycling from outward- to inward-open states, efficient proton transport still occurs in outward-locked (but not inward-locked) DraNramp. We propose a model in which metal and proton enter the transporter via the same external pathway to the binding site, but follow separate routes to the cytoplasm, which could facilitate the co-transport of two cationic species. Our results illustrate the flexibility of the LeuT fold to support a broad range of substrate transport and conformational change mechanisms.

PubMed: 30714568
DOI: 10.7554/eLife.41124

実験手法

X-RAY DIFFRACTION (3.941 Å)