6Z16

Structure of the Mrp antiporter complex

6Z16 の概要

• エントリーDOI: 10.2210/pdb6z16/pdb
• EMDBエントリー: 11027
• 分子名称: Multisubunit Na+/H+ antiporter, A subunit, Multisubunit Na+/H+ antiporter, B subunit, Multisubunit Na+/H+ antiporter, C subunit, ... (9 entities in total)
• 機能のキーワード: mrp antiporter, sodium/proton exchanger, bioenergetics, complex, membrane protein
• 由来する生物種: Anoxybacillus flavithermus (strain DSM 21510 / WK1); 詳細
• タンパク質・核酸の鎖数: 14
• 化学式量合計: 446182.56

構造登録者

Steiner, J.,Sazanov, L.A. (登録日: 2020-05-12, 公開日: 2020-08-12, 最終更新日: 2024-05-22)

主引用文献

Steiner, J.,Sazanov, L.
Structure and mechanism of the Mrp complex, an ancient cation/proton antiporter.
Elife, 9:-, 2020

PubMed Abstract: Multiple resistance and pH adaptation (Mrp) antiporters are multi-subunit Na (or K)/H exchangers representing an ancestor of many essential redox-driven proton pumps, such as respiratory complex I. The mechanism of coupling between ion or electron transfer and proton translocation in this large protein family is unknown. Here, we present the structure of the Mrp complex from solved by cryo-EM at 3.0 Å resolution. It is a dimer of seven-subunit protomers with 50 trans-membrane helices each. Surface charge distribution within each monomer is remarkably asymmetric, revealing probable proton and sodium translocation pathways. On the basis of the structure we propose a mechanism where the coupling between sodium and proton translocation is facilitated by a series of electrostatic interactions between a cation and key charged residues. This mechanism is likely to be applicable to the entire family of redox proton pumps, where electron transfer to substrates replaces cation movements.

PubMed: 32735215
DOI: 10.7554/eLife.59407

実験手法

ELECTRON MICROSCOPY (2.98 Å)