5BZ2

CRYSTAL STRUCTURE OF THE SODIUM PROTON ANTIPORTER NAPA IN INWARD-FACING CONFORMATION

5BZ2 の概要

• エントリーDOI: 10.2210/pdb5bz2/pdb
• 分子名称: Na(+)/H(+) antiporter (1 entity in total)
• 機能のキーワード: transport protein, inward-facing, cystein crosslink
• 由来する生物種: Thermus thermophilus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 40306.11

構造登録者

Coincon, M.,Uzdavinys, P.,Cameron, A.,Drew, D. (登録日: 2015-06-11, 公開日: 2016-01-20, 最終更新日: 2024-01-10)

主引用文献

Coincon, M.,Uzdavinys, P.,Nji, E.,Dotson, D.L.,Winkelmann, I.,Abdul-Hussein, S.,Cameron, A.D.,Beckstein, O.,Drew, D.
Crystal structures reveal the molecular basis of ion translocation in sodium/proton antiporters.
Nat.Struct.Mol.Biol., 23:248-255, 2016

PubMed Abstract: To fully understand the transport mechanism of Na(+)/H(+) exchangers, it is necessary to clearly establish the global rearrangements required to facilitate ion translocation. Currently, two different transport models have been proposed. Some reports have suggested that structural isomerization is achieved through large elevator-like rearrangements similar to those seen in the structurally unrelated sodium-coupled glutamate-transporter homolog GltPh. Others have proposed that only small domain movements are required for ion exchange, and a conventional rocking-bundle model has been proposed instead. Here, to resolve these differences, we report atomic-resolution structures of the same Na(+)/H(+) antiporter (NapA from Thermus thermophilus) in both outward- and inward-facing conformations. These data combined with cross-linking, molecular dynamics simulations and isothermal calorimetry suggest that Na(+)/H(+) antiporters provide alternating access to the ion-binding site by using elevator-like structural transitions.

PubMed: 26828964
DOI: 10.1038/nsmb.3164

実験手法

X-RAY DIFFRACTION (3.7 Å)