7D3U

Structure of Mrp complex from Dietzia sp. DQ12-45-1b

7D3U の概要

• エントリーDOI: 10.2210/pdb7d3u/pdb
• EMDBエントリー: 30567
• 分子名称: Monovalent Na+/H+ antiporter subunit D, Monovalent Na+/H+ antiporter subunit A, Monovalent Na+/H+ antiporter subunit C, ... (7 entities in total)
• 機能のキーワード: sodium/proton antiporter, membrane protein
• 由来する生物種: Dietzia sp. DQ12-45-1b; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 223353.39

構造登録者

Li, B.,Zhang, K.D.,Wu, X.L.,Zhang, X.C. (登録日: 2020-09-21, 公開日: 2020-12-09, 最終更新日: 2024-03-27)

主引用文献

Li, B.,Zhang, K.,Nie, Y.,Wang, X.,Zhao, Y.,Zhang, X.C.,Wu, X.L.
Structure of the Dietzia Mrp complex reveals molecular mechanism of this giant bacterial sodium proton pump.
Proc.Natl.Acad.Sci.USA, 117:31166-31176, 2020

PubMed Abstract: Multiple resistance and pH adaptation (Mrp) complexes are sophisticated cation/proton exchangers found in a vast variety of alkaliphilic and/or halophilic microorganisms, and are critical for their survival in highly challenging environments. This family of antiporters is likely to represent the ancestor of cation pumps found in many redox-driven transporter complexes, including the complex I of the respiratory chain. Here, we present the three-dimensional structure of the Mrp complex from a sp. strain solved at 3.0-Å resolution using the single-particle cryoelectron microscopy method. Our structure-based mutagenesis and functional analyses suggest that the substrate translocation pathways for the driving substance protons and the substrate sodium ions are separated in two modules and that symmetry-restrained conformational change underlies the functional cycle of the transporter. Our findings shed light on mechanisms of redox-driven primary active transporters, and explain how driving substances of different electric charges may drive similar transport processes.

PubMed: 33229520
DOI: 10.1073/pnas.2006276117

実験手法

ELECTRON MICROSCOPY (3 Å)