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Yorodumi- EMDB-15693: Structure of Bacillus pseudofirmus Mrp antiporter complex, monome... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-15693 | |||||||||
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Title | Structure of Bacillus pseudofirmus Mrp antiporter complex, monomer, processed at original pixel size (0.837 A/pix) | |||||||||
Map data | ||||||||||
Sample |
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Biological species | Alkalihalobacillus pseudofirmus (bacteria) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.25 Å | |||||||||
Authors | Lee Y | |||||||||
Funding support | Germany, 1 items
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Citation | Journal: Nat Commun / Year: 2022 Title: Ion transfer mechanisms in Mrp-type antiporters from high resolution cryoEM and molecular dynamics simulations. Authors: Yongchan Lee / Outi Haapanen / Anton Altmeyer / Werner Kühlbrandt / Vivek Sharma / Volker Zickermann / Abstract: Multiple resistance and pH adaptation (Mrp) cation/proton antiporters are essential for growth of a variety of halophilic and alkaliphilic bacteria under stress conditions. Mrp-type antiporters are ...Multiple resistance and pH adaptation (Mrp) cation/proton antiporters are essential for growth of a variety of halophilic and alkaliphilic bacteria under stress conditions. Mrp-type antiporters are closely related to the membrane domain of respiratory complex I. We determined the structure of the Mrp antiporter from Bacillus pseudofirmus by electron cryo-microscopy at 2.2 Å resolution. The structure resolves more than 99% of the sidechains of the seven membrane subunits MrpA to MrpG plus 360 water molecules, including ~70 in putative ion translocation pathways. Molecular dynamics simulations based on the high-resolution structure revealed details of the antiport mechanism. We find that switching the position of a histidine residue between three hydrated pathways in the MrpA subunit is critical for proton transfer that drives gated trans-membrane sodium translocation. Several lines of evidence indicate that the same histidine-switch mechanism operates in respiratory complex I. | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_15693.map.gz | 27.4 MB | EMDB map data format | |
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Header (meta data) | emd-15693-v30.xml emd-15693.xml | 13.5 KB 13.5 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_15693_fsc.xml | 18 KB | Display | FSC data file |
Images | emd_15693.png | 97.3 KB | ||
Masks | emd_15693_msk_1.map | 512 MB | Mask map | |
Others | emd_15693_half_map_1.map.gz emd_15693_half_map_2.map.gz | 414 MB 414 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-15693 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-15693 | HTTPS FTP |
-Validation report
Summary document | emd_15693_validation.pdf.gz | 630.6 KB | Display | EMDB validaton report |
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Full document | emd_15693_full_validation.pdf.gz | 630.2 KB | Display | |
Data in XML | emd_15693_validation.xml.gz | 25.3 KB | Display | |
Data in CIF | emd_15693_validation.cif.gz | 34.1 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-15693 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-15693 | HTTPS FTP |
-Related structure data
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_15693.map.gz / Format: CCP4 / Size: 512 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.837 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
File | emd_15693_msk_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_15693_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_15693_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
-Entire : MrpABCDEFG complex
Entire | Name: MrpABCDEFG complex |
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Components |
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-Supramolecule #1: MrpABCDEFG complex
Supramolecule | Name: MrpABCDEFG complex / type: complex / Chimera: Yes / ID: 1 / Parent: 0 / Macromolecule list: #1-#7 |
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Source (natural) | Organism: Alkalihalobacillus pseudofirmus (bacteria) |
Recombinant expression | Organism: Escherichia coli (E. coli) |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 8 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.8 µm |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |