[English] 日本語
Yorodumi- EMDB-14124: Structure of Bacillus pseudofirmus Mrp antiporter complex, monomer -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-14124 | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | Structure of Bacillus pseudofirmus Mrp antiporter complex, monomer | |||||||||
Map data | ||||||||||
Sample |
| |||||||||
Function / homology | Function and homology information : / monoatomic ion transmembrane transporter activity / antiporter activity / inorganic cation transmembrane transport / monoatomic cation transmembrane transporter activity / sodium ion transport / NADH dehydrogenase (ubiquinone) activity / ATP synthesis coupled electron transport / monoatomic ion transport / proton transmembrane transport ...: / monoatomic ion transmembrane transporter activity / antiporter activity / inorganic cation transmembrane transport / monoatomic cation transmembrane transporter activity / sodium ion transport / NADH dehydrogenase (ubiquinone) activity / ATP synthesis coupled electron transport / monoatomic ion transport / proton transmembrane transport / membrane => GO:0016020 / plasma membrane Similarity search - Function | |||||||||
Biological species | Alkalihalobacillus pseudofirmus (bacteria) / Alkalihalophilus pseudofirmus (bacteria) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.24 Å | |||||||||
Authors | Lee Y | |||||||||
Funding support | Germany, 1 items
| |||||||||
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 |
|
-Structure visualization
Supplemental images |
---|
-Downloads & links
-EMDB archive
Map data | emd_14124.map.gz | 10.9 MB | EMDB map data format | |
---|---|---|---|---|
Header (meta data) | emd-14124-v30.xml emd-14124.xml | 21.9 KB 21.9 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_14124_fsc.xml | 14 KB | Display | FSC data file |
Images | emd_14124.png | 91.2 KB | ||
Masks | emd_14124_msk_1.map | 244.1 MB | Mask map | |
Others | emd_14124_half_map_1.map.gz emd_14124_half_map_2.map.gz | 194.7 MB 194.7 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-14124 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-14124 | HTTPS FTP |
-Related structure data
Related structure data | 7qruMC M: atomic model generated by this map C: citing same article (ref.) |
---|---|
Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
---|---|
Related items in Molecule of the Month |
-Map
File | Download / File: emd_14124.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.07136 Å | ||||||||||||||||||||||||||||||||||||
Density |
| ||||||||||||||||||||||||||||||||||||
Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
|
-Supplemental data
-Mask #1
File | emd_14124_msk_1.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Projections & Slices |
| ||||||||||||
Density Histograms |
-Half map: #2
File | emd_14124_half_map_1.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Projections & Slices |
| ||||||||||||
Density Histograms |
-Half map: #1
File | emd_14124_half_map_2.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Projections & Slices |
| ||||||||||||
Density Histograms |
-Sample components
+Entire : MrpABCDEFG complex
+Supramolecule #1: MrpABCDEFG complex
+Macromolecule #1: Na+/H+ antiporter subunit D
+Macromolecule #2: Na+/H+ antiporter subunit A
+Macromolecule #3: Na(+)/H(+) antiporter subunit B
+Macromolecule #4: Na(+)/H(+) antiporter subunit C
+Macromolecule #5: Na+/H+ antiporter subunit E
+Macromolecule #6: Na(+)/H(+) antiporter subunit F
+Macromolecule #7: Na+/H+ antiporter subunit G1
+Macromolecule #8: 1,2-Distearoyl-sn-glycerophosphoethanolamine
+Macromolecule #9: water
-Experimental details
-Structure determination
Method | cryo EM |
---|---|
Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 8 |
---|---|
Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
---|---|
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.8 µm |
Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2 |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |