+Open data
-Basic information
Entry | Database: PDB / ID: 7d3u | |||||||||
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Title | Structure of Mrp complex from Dietzia sp. DQ12-45-1b | |||||||||
Components |
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Keywords | MEMBRANE PROTEIN / Sodium/proton antiporter | |||||||||
Function / homology | Function and homology information : / monoatomic ion transmembrane transporter activity / monoatomic cation transmembrane transporter activity / NADH dehydrogenase (ubiquinone) activity / ATP synthesis coupled electron transport / membrane => GO:0016020 / plasma membrane Similarity search - Function | |||||||||
Biological species | Dietzia sp. DQ12-45-1b (bacteria) | |||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3 Å | |||||||||
Authors | Li, B. / Zhang, K.D. / Wu, X.L. / Zhang, X.C. | |||||||||
Funding support | China, 2items
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Citation | Journal: Proc Natl Acad Sci U S A / Year: 2020 Title: Structure of the Mrp complex reveals molecular mechanism of this giant bacterial sodium proton pump. Authors: Bin Li / Kaiduan Zhang / Yong Nie / Xianping Wang / Yan Zhao / Xuejun C Zhang / Xiao-Lei Wu / 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 ...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. | |||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | Molecule: MolmilJmol/JSmol |
-Downloads & links
-Download
PDBx/mmCIF format | 7d3u.cif.gz | 330 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7d3u.ent.gz | 262.3 KB | Display | PDB format |
PDBx/mmJSON format | 7d3u.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/d3/7d3u ftp://data.pdbj.org/pub/pdb/validation_reports/d3/7d3u | HTTPS FTP |
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-Related structure data
Related structure data | 30567MC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
-Monovalent Na+/H+ antiporter subunit ... , 5 types, 5 molecules DACFG
#1: Protein | Mass: 59028.000 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Dietzia sp. DQ12-45-1b (bacteria) / Gene: amnhD, GJR88_00771 / Production host: Escherichia coli (E. coli) / References: UniProt: A0A221C8X0 |
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#2: Protein | Mass: 100097.484 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Dietzia sp. DQ12-45-1b (bacteria) / Gene: amnhA, GJR88_00777 / Production host: Escherichia coli (E. coli) / References: UniProt: A0A221C8X2 |
#3: Protein | Mass: 14310.331 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Dietzia sp. DQ12-45-1b (bacteria) / Gene: amnhC, GJR88_00774 / Production host: Escherichia coli (E. coli) / References: UniProt: A0A221C8X5 |
#4: Protein | Mass: 8960.800 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Dietzia sp. DQ12-45-1b (bacteria) / Gene: amnhF, GJR88_00768 / Production host: Escherichia coli (E. coli) / References: UniProt: A0A221C8X7 |
#5: Protein | Mass: 12780.665 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Dietzia sp. DQ12-45-1b (bacteria) / Gene: amnhG, GJR88_00766 / Production host: Escherichia coli (E. coli) / References: UniProt: A0A221C8Y4 |
-Protein / Sugars , 2 types, 29 molecules E
#6: Protein | Mass: 13878.893 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Dietzia sp. DQ12-45-1b (bacteria) / Gene: amnhE, GJR88_00770 / Production host: Escherichia coli (E. coli) / References: UniProt: A0A221C8X1 |
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#7: Sugar | ChemComp-LMT / |
-Details
Has ligand of interest | N |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-Sample preparation
Component | Name: Mrp complex of Dietzia sp. DQ12-45-1b / Type: COMPLEX / Entity ID: #1-#6 / Source: RECOMBINANT |
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Source (natural) | Organism: Dietzia sp. DQ12-45-1b (bacteria) |
Source (recombinant) | Organism: Escherichia coli (E. coli) |
Buffer solution | pH: 7.5 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Specimen support | Grid material: COPPER |
Vitrification | Cryogen name: ETHANE |
-Electron microscopy imaging
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
Electron lens | Mode: BRIGHT FIELDBright-field microscopy |
Image recording | Electron dose: 60 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
-Processing
Software | Name: PHENIX / Version: 1.17.1_3660: / Classification: refinement | ||||||||||||||||||||||||
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
3D reconstruction | Resolution: 3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 93505 / Symmetry type: POINT | ||||||||||||||||||||||||
Refine LS restraints |
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