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-Structure paper
タイトル | Structure of the Mrp complex reveals molecular mechanism of this giant bacterial sodium proton pump. |
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ジャーナル・号・ページ | Proc Natl Acad Sci U S A, Vol. 117, Issue 49, Page 31166-31176, Year 2020 |
掲載日 | 2020年12月8日 |
![]() | Bin Li / Kaiduan Zhang / Yong Nie / Xianping Wang / Yan Zhao / Xuejun C Zhang / Xiao-Lei Wu / ![]() |
PubMed 要旨 | 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 ...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. |
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手法 | EM (単粒子) |
解像度 | 3.0 Å |
構造データ | EMDB-30567, PDB-7d3u: |
化合物 | ![]() ChemComp-LMT: |
由来 |
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![]() | MEMBRANE PROTEIN / Sodium/proton antiporter |