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Open data
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Basic information
Entry | Database: PDB / ID: 5wua | |||||||||
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Title | Structure of a Pancreatic ATP-sensitive Potassium Channel | |||||||||
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![]() | TRANSPORT PROTEIN / KATP / channel / ABC transporter / Kir | |||||||||
Function / homology | ![]() ATP sensitive Potassium channels / response to resveratrol / ATP-activated inward rectifier potassium channel activity / inward rectifying potassium channel / Regulation of insulin secretion / sulfonylurea receptor activity / cell body fiber / ventricular cardiac muscle tissue development / ABC-family proteins mediated transport / CAMKK-AMPK signaling cascade ...ATP sensitive Potassium channels / response to resveratrol / ATP-activated inward rectifier potassium channel activity / inward rectifying potassium channel / Regulation of insulin secretion / sulfonylurea receptor activity / cell body fiber / ventricular cardiac muscle tissue development / ABC-family proteins mediated transport / CAMKK-AMPK signaling cascade / inward rectifier potassium channel activity / voltage-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential / Ion homeostasis / ATPase-coupled monoatomic cation transmembrane transporter activity / nervous system process / inorganic cation transmembrane transport / ankyrin binding / response to ATP / response to stress / potassium ion import across plasma membrane / response to testosterone / potassium ion binding / action potential / intercalated disc / axolemma / negative regulation of insulin secretion / cellular response to nutrient levels / ABC-type transporter activity / T-tubule / heat shock protein binding / acrosomal vesicle / response to ischemia / determination of adult lifespan / positive regulation of protein localization to plasma membrane / cellular response to glucose stimulus / potassium ion transport / cellular response to nicotine / glucose metabolic process / nuclear envelope / cellular response to tumor necrosis factor / response to estradiol / presynaptic membrane / transmembrane transporter binding / response to hypoxia / endosome / response to xenobiotic stimulus / neuronal cell body / apoptotic process / glutamatergic synapse / protein-containing complex / ATP hydrolysis activity / ATP binding / plasma membrane / cytoplasm Similarity search - Function | |||||||||
Biological species | ![]() ![]() synthetic construct (others) ![]() | |||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 5.6 Å | |||||||||
![]() | Li, N. / Wu, J.-X. / Chen, L. / Gao, N. | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Structure of a Pancreatic ATP-Sensitive Potassium Channel. Authors: Ningning Li / Jing-Xiang Wu / Dian Ding / Jiaxuan Cheng / Ning Gao / Lei Chen / ![]() Abstract: ATP-sensitive potassium channels (K) couple intracellular ATP levels with membrane excitability. These channels play crucial roles in many essential physiological processes and have been implicated ...ATP-sensitive potassium channels (K) couple intracellular ATP levels with membrane excitability. These channels play crucial roles in many essential physiological processes and have been implicated extensively in a spectrum of metabolic diseases and disorders. To gain insight into the mechanism of K, we elucidated the structure of a hetero-octameric pancreatic K channel in complex with a non-competitive inhibitor glibenclamide by single-particle cryoelectron microscopy to 5.6-Å resolution. The structure shows that four SUR1 regulatory subunits locate peripherally and dock onto the central Kir6.2 channel tetramer through the SUR1 TMD0-L0 fragment. Glibenclamide-bound SUR1 uses TMD0-L0 fragment to stabilize Kir6.2 channel in a closed conformation. In another structural population, a putative co-purified phosphatidylinositol 4,5-bisphosphate (PIP) molecule uncouples Kir6.2 from glibenclamide-bound SUR1. These structural observations suggest a molecular mechanism for K regulation by anti-diabetic sulfonylurea drugs, intracellular adenosine nucleotide concentrations, and PIP lipid. | |||||||||
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Structure visualization
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Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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PDBx/mmCIF format | ![]() | 959.6 KB | Display | ![]() |
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PDB format | ![]() | 681.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 1.2 MB | Display | ![]() |
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Full document | ![]() | 1.4 MB | Display | |
Data in XML | ![]() | 171.5 KB | Display | |
Data in CIF | ![]() | 260.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6689MC M: map data used to model this data C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Components
#1: Protein | Mass: 76339.242 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Details: ATP-sensitive inward rectifier potassium channel 11 with C-terminal synthetic superfolder GFP and affinity tags added Source: (gene. exp.) ![]() ![]() Gene: Kcnj11 / Cell line (production host): HEK / Production host: ![]() #2: Protein | Mass: 177296.578 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Has protein modification | Y | |
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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 |
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Sample preparation
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Molecular weight | Value: 880 kDa/nm / Experimental value: NO | ||||||||||||||||||||||||
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Buffer solution | pH: 7.5 | ||||||||||||||||||||||||
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||
Vitrification | Cryogen name: ETHANE |
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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: ![]() |
Electron lens | Mode: BRIGHT FIELD |
Image recording | Electron dose: 40 e/Å2 / Detector mode: INTEGRATING / Film or detector model: FEI FALCON II (4k x 4k) |
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Processing
EM software | Name: RELION / Version: 2 / Category: 3D reconstruction |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
Symmetry | Point symmetry: C4 (4 fold cyclic) |
3D reconstruction | Resolution: 5.6 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 34500 / Symmetry type: POINT |