首页    期刊浏览 2024年12月12日 星期四
登录注册

文章基本信息

  • 标题:Structure of the Dietzia Mrp complex reveals molecular mechanism of this giant bacterial sodium proton pump
  • 本地全文:下载
  • 作者:Bin Li ; Kaiduan Zhang ; Yong Nie
  • 期刊名称:Proceedings of the National Academy of Sciences
  • 印刷版ISSN:0027-8424
  • 电子版ISSN:1091-6490
  • 出版年度:2020
  • 卷号:117
  • 期号:49
  • 页码:31166-31176
  • DOI:10.1073/pnas.2006276117
  • 出版社:The National Academy of Sciences of the United States of America
  • 摘要: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 Dietzia 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.
  • 关键词:Na /H antiporter ; Mrp complex ; cryo-EM ; complex I ; energy coupling
国家哲学社会科学文献中心版权所有