[English] 日本語
Yorodumi- EMDB-55889: Cryo-EM structure of the R162W mutant inward rectifying potassium... -
+
Open data
-
Basic information
| Entry | ![]() | |||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| Title | Cryo-EM structure of the R162W mutant inward rectifying potassium channel 7.1 (Kir7.1) | |||||||||
Map data | ||||||||||
Sample |
| |||||||||
Keywords | potassium ion channel / active conformation / human membrane protein / MEMBRANE PROTEIN | |||||||||
| Function / homology | Function and homology informationinward rectifier potassium channel activity / regulation of monoatomic ion transmembrane transport / potassium ion import across plasma membrane / monoatomic ion channel complex / potassium ion transport / regulation of membrane potential / plasma membrane Similarity search - Function | |||||||||
| Biological species | Homo sapiens (human) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.5 Å | |||||||||
Authors | O'Malley N / Faust B / Nasrallah C / Wallace BA | |||||||||
| Funding support | United Kingdom, 1 items
| |||||||||
Citation | Journal: Commun Biol / Year: 2026Title: Cryo-EM structure of the human Kir7.1 channel reveals the molecular basis of snowflake vitreoretinal degeneration disease. Authors: Niamh O'Malley / Chady Nasrallah / Ashton Churchill / Jay Bertrand / Belinda R Faust / B A Wallace / ![]() Abstract: The inward rectifying human potassium channel 7.1 (Kir7.1) is a vital ion channel involved in maintaining cellular homoeostasis and electrical signalling across various tissues and organs, activated ...The inward rectifying human potassium channel 7.1 (Kir7.1) is a vital ion channel involved in maintaining cellular homoeostasis and electrical signalling across various tissues and organs, activated by phosphatidylinositol 4,5-bisphosphate (PIP). A genetically inherited loss-of-function mutation in Kir7.1 (R162W) has been linked to the rare retinal disease Snowflake Vitreoretinal Degeneration (SVD), for which there are currently no curative treatment options. Here, the cryo-EM structures of wild type Kir7.1 and the R162W disease-related variant are presented, which unveil the molecular basis of SVD: the reorientation of the mutant tryptophan side chains into the pore impedes the flow of potassium ions, which would result in the loss of Kir7.1 transport function. Furthermore, this investigation shows that PIP binding widens the helix bundle crossing gate diameter, even in the absence of a docked cytoplasmic domain. This observation contrasts with other Kir-PIP₂ complexes and suggests that Kir7.1 may adopt an intermediate conformation during channel activation. These findings provide a structural basis for Kir7.1 loss of function in SVD and provide a framework for future therapeutic development. | |||||||||
| History |
|
-
Structure visualization
| Supplemental images |
|---|
-
Downloads & links
-EMDB archive
| Map data | emd_55889.map.gz | 306 MB | EMDB map data format | |
|---|---|---|---|---|
| Header (meta data) | emd-55889-v30.xml emd-55889.xml | 19.1 KB 19.1 KB | Display Display | EMDB header |
| Images | emd_55889.png | 43.8 KB | ||
| Filedesc metadata | emd-55889.cif.gz | 6.3 KB | ||
| Others | emd_55889_half_map_1.map.gz emd_55889_half_map_2.map.gz | 301.1 MB 301.1 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-55889 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-55889 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9tg3MC ![]() 9tfvC ![]() 9tg6C M: atomic model generated by this map C: citing same article ( |
|---|---|
| Similar structure data | Similarity search - Function & homology F&H Search |
-
Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
|---|
-
Map
| File | Download / File: emd_55889.map.gz / Format: CCP4 / Size: 325 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.65 Å | ||||||||||||||||||||||||||||||||||||
| Density |
| ||||||||||||||||||||||||||||||||||||
| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
|
-Supplemental data
-Half map: #2
| File | emd_55889_half_map_1.map | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Projections & Slices |
| ||||||||||||
| Density Histograms |
-Half map: #1
| File | emd_55889_half_map_2.map | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Projections & Slices |
| ||||||||||||
| Density Histograms |
-
Sample components
-Entire : Tetrameric assembly of human inward rectifying potassium channel 7.1
| Entire | Name: Tetrameric assembly of human inward rectifying potassium channel 7.1 |
|---|---|
| Components |
|
-Supramolecule #1: Tetrameric assembly of human inward rectifying potassium channel 7.1
| Supramolecule | Name: Tetrameric assembly of human inward rectifying potassium channel 7.1 type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
|---|---|
| Source (natural) | Organism: Homo sapiens (human) |
-Macromolecule #1: Inward rectifier potassium channel 13
| Macromolecule | Name: Inward rectifier potassium channel 13 / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO |
|---|---|
| Source (natural) | Organism: Homo sapiens (human) |
| Molecular weight | Theoretical: 42.534406 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: DYKDDDDKGS MDSSNCKVIA PLLSQRYRRM VTKDGHSTLQ MDGAQRGLAY LRDAWGILMD MRWRWMMLVF SASFVVHWLV FAVLWYVLA EMNGDLELDH DAPPENHTIC VKYITSFTAA FSFSLETQLT IGYGTMFPSG DCPSAIALLA IQMLLGLMLE A FITGAFVA ...String: DYKDDDDKGS MDSSNCKVIA PLLSQRYRRM VTKDGHSTLQ MDGAQRGLAY LRDAWGILMD MRWRWMMLVF SASFVVHWLV FAVLWYVLA EMNGDLELDH DAPPENHTIC VKYITSFTAA FSFSLETQLT IGYGTMFPSG DCPSAIALLA IQMLLGLMLE A FITGAFVA KIAWPKNRAF SIRFTDTAVV AHMDGKPNLI FQVANTRPSP LTSVRVSAVL YQERENGKLY QTSVDFHLDG IS SDECPFF IFPLTYYHSI TPSSPLATLL QHENPSHFEL VVFLSAMQEG TGEICQRRTS YLPSEIMLHH CFASLLTRGS KGE YQIKME NFDKTVPEFP TPLVSKSPNR TDLDIHINGQ SIDNFQISET GLTEENLYFQ UniProtKB: Inward rectifier potassium channel 13 |
-Macromolecule #2: POTASSIUM ION
| Macromolecule | Name: POTASSIUM ION / type: ligand / ID: 2 / Number of copies: 2 / Formula: K |
|---|---|
| Molecular weight | Theoretical: 39.098 Da |
-Experimental details
-Structure determination
| Method | cryo EM |
|---|---|
Processing | single particle reconstruction |
| Aggregation state | particle |
-
Sample preparation
| Concentration | 6 mg/mL |
|---|---|
| Buffer | pH: 7.5 |
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV |
-
Electron microscopy
| Microscope | TFS KRIOS |
|---|---|
| Image recording | Film or detector model: GATAN K3 (6k x 4k) / Number real images: 22098 / Average electron dose: 31.9 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: 2.7 µm / Nominal defocus min: 1.2 µm |
| Sample stage | Cooling holder cryogen: NITROGEN |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
+
Image processing
-Atomic model buiding 1
| Initial model | Chain - Source name: Other / Chain - Initial model type: in silico model / Details: ModelAngelo |
|---|---|
| Refinement | Protocol: AB INITIO MODEL |
| Output model | ![]() PDB-9tg3: |
Movie
Controller
About Yorodumi



Keywords
Homo sapiens (human)
Authors
United Kingdom, 1 items
Citation





Z (Sec.)
Y (Row.)
X (Col.)




































FIELD EMISSION GUN
