7D3U
Structure of Mrp complex from Dietzia sp. DQ12-45-1b
Summary for 7D3U
| Entry DOI | 10.2210/pdb7d3u/pdb |
| EMDB information | 30567 |
| Descriptor | Monovalent Na+/H+ antiporter subunit D, Monovalent Na+/H+ antiporter subunit A, Monovalent Na+/H+ antiporter subunit C, ... (7 entities in total) |
| Functional Keywords | sodium/proton antiporter, membrane protein |
| Biological source | Dietzia sp. DQ12-45-1b More |
| Total number of polymer chains | 6 |
| Total formula weight | 223353.39 |
| Authors | Li, B.,Zhang, K.D.,Wu, X.L.,Zhang, X.C. (deposition date: 2020-09-21, release date: 2020-12-09, Last modification date: 2024-03-27) |
| Primary citation | 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 Cited by 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: 33229520DOI: 10.1073/pnas.2006276117 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3 Å) |
Structure validation
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