4D0A

3D EM map of the sodium proton antiporter MjNhaP1 from Methanocaldococcus jannaschii

4D0A の概要

• エントリーDOI: 10.2210/pdb4d0a/pdb
• EMDBエントリー: 2636
• 分子名称: NA(+)/H(+) ANTIPORTER 1 (1 entity in total)
• 機能のキーワード: transport protein, membrane protein, antiporter, transporter, exchanger, cpa
• 由来する生物種: METHANOCALDOCOCCUS JANNASCHII DSM 2661
• 細胞内の位置: Cell membrane ; Multi-pass membrane protein : Q60362
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 45998.89

構造登録者

Paulino, C.,Woehlert, D.,Yildiz, O.,Kuhlbrandt, W. (登録日: 2014-04-25, 公開日: 2014-12-10, 最終更新日: 2023-12-20)

主引用文献

Paulino, C.,Woehlert, D.,Yildiz, O.,Kuhlbrandt, W.
3D Em Map of the Sodium Proton Antiporter Mjnhap1 from Methanocaldococcus Jannaschii
Elife, 3:-, 2014

PubMed Abstract: Sodium/proton antiporters are essential for sodium and pH homeostasis and play a major role in human health and disease. We determined the structures of the archaeal sodium/proton antiporter MjNhaP1 in two complementary states. The inward-open state was obtained by x-ray crystallography in the presence of sodium at pH 8, where the transporter is highly active. The outward-open state was obtained by electron crystallography without sodium at pH 4, where MjNhaP1 is inactive. Comparison of both structures reveals a 7° tilt of the 6 helix bundle. (22)Na(+) uptake measurements indicate non-cooperative transport with an activity maximum at pH 7.5. We conclude that binding of a Na(+) ion from the outside induces helix movements that close the extracellular cavity, open the cytoplasmic funnel, and result in a ∼5 Å vertical relocation of the ion binding site to release the substrate ion into the cytoplasm.

PubMed: 25426803
DOI: 10.7554/ELIFE.03583

実験手法

ELECTRON CRYSTALLOGRAPHY (6 Å)