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Yorodumi- PDB-5ykg: Structure of pancreatic ATP-sensitive potassium channel bound wit... -
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-Basic information
Entry | Database: PDB / ID: 5ykg | ||||||||||||||||||
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Title | Structure of pancreatic ATP-sensitive potassium channel bound with glibenclamide and ATPgammaS (Class2 at 4.57A) | ||||||||||||||||||
Components |
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Keywords | MEMBRANE PROTEIN / KATP / channel / glibenclamide / sulfonylurea | ||||||||||||||||||
Function / homology | Function and homology information ATP sensitive Potassium channels / response to resveratrol / ATP-activated inward rectifier potassium channel activity / glutamate secretion, neurotransmission / inward rectifying potassium channel / Regulation of insulin secretion / sulfonylurea receptor activity / cell body fiber / ventricular cardiac muscle tissue development / ABC-family proteins mediated transport ...ATP sensitive Potassium channels / response to resveratrol / ATP-activated inward rectifier potassium channel activity / glutamate secretion, neurotransmission / 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 / voltage-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential / Ion homeostasis / ATPase-coupled monoatomic cation transmembrane transporter activity / inward rectifier potassium channel activity / regulation of monoatomic ion transmembrane transport / nervous system process / inorganic cation transmembrane transport / response to stress / ankyrin binding / neuromuscular process / response to ATP / action potential / potassium ion import across plasma membrane / response to testosterone / positive regulation of insulin secretion involved in cellular response to glucose stimulus / potassium ion binding / intercalated disc / potassium channel activity / axolemma / ABC-type transporter activity / negative regulation of insulin secretion / cellular response to nutrient levels / heat shock protein binding / T-tubule / acrosomal vesicle / determination of adult lifespan / response to ischemia / positive regulation of protein localization to plasma membrane / cellular response to glucose stimulus / ADP binding / potassium ion transport / sarcolemma / cellular response to nicotine / glucose metabolic process / cellular response to tumor necrosis factor / nuclear envelope / response to estradiol / presynapse / presynaptic membrane / transmembrane transporter binding / response to hypoxia / endosome / response to xenobiotic stimulus / neuronal cell body / glutamatergic synapse / apoptotic process / ATP hydrolysis activity / ATP binding / plasma membrane / cytoplasm Similarity search - Function | ||||||||||||||||||
Biological species | Mus musculus (house mouse) Mesocricetus auratus (golden hamster) | ||||||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.57 Å | ||||||||||||||||||
Authors | Chen, L. / Wu, J.X. | ||||||||||||||||||
Funding support | China, 5items
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Citation | Journal: Protein Cell / Year: 2018 Title: Ligand binding and conformational changes of SUR1 subunit in pancreatic ATP-sensitive potassium channels. Authors: Jing-Xiang Wu / Dian Ding / Mengmeng Wang / Yunlu Kang / Xin Zeng / Lei Chen / Abstract: ATP-sensitive potassium channels (K) are energy sensors on the plasma membrane. By sensing the intracellular ADP/ATP ratio of β-cells, pancreatic K channels control insulin release and regulate ...ATP-sensitive potassium channels (K) are energy sensors on the plasma membrane. By sensing the intracellular ADP/ATP ratio of β-cells, pancreatic K channels control insulin release and regulate metabolism at the whole body level. They are implicated in many metabolic disorders and diseases and are therefore important drug targets. Here, we present three structures of pancreatic K channels solved by cryo-electron microscopy (cryo-EM), at resolutions ranging from 4.1 to 4.5 Å. These structures depict the binding site of the antidiabetic drug glibenclamide, indicate how Kir6.2 (inward-rectifying potassium channel 6.2) N-terminus participates in the coupling between the peripheral SUR1 (sulfonylurea receptor 1) subunit and the central Kir6.2 channel, reveal the binding mode of activating nucleotides, and suggest the mechanism of how Mg-ADP binding on nucleotide binding domains (NBDs) drives a conformational change of the SUR1 subunit. | ||||||||||||||||||
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 | 5ykg.cif.gz | 1.2 MB | Display | PDBx/mmCIF format |
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PDB format | pdb5ykg.ent.gz | 1013.6 KB | Display | PDB format |
PDBx/mmJSON format | 5ykg.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5ykg_validation.pdf.gz | 1.9 MB | Display | wwPDB validaton report |
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Full document | 5ykg_full_validation.pdf.gz | 2 MB | Display | |
Data in XML | 5ykg_validation.xml.gz | 185.6 KB | Display | |
Data in CIF | 5ykg_validation.cif.gz | 270.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/yk/5ykg ftp://data.pdbj.org/pub/pdb/validation_reports/yk/5ykg | HTTPS FTP |
-Related structure data
Related structure data | 6833MC 6831C 6832C 6847C 6848C 6849C 6850C 6851C 6852C 6853C 5ykeC 5ykfC 5yw7C 5yw8C 5yw9C 5ywaC 5ywbC 5ywcC 5ywdC 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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-Components
#1: Protein | Mass: 43615.734 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Kcnj11 / Production host: Homo sapiens (human) / References: UniProt: Q61743 #2: Protein | Mass: 177295.516 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mesocricetus auratus (golden hamster) / Gene: Abcc8 / Production host: Homo sapiens (human) / References: UniProt: A0A1U7R319 #3: Chemical | ChemComp-AGS / #4: Chemical | ChemComp-GBM / |
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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: KATP / Type: COMPLEX / Entity ID: #1-#2 / Source: RECOMBINANT |
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Source (natural) | Organism: Mus musculus (house mouse) |
Source (recombinant) | Organism: Homo sapiens (human) |
Buffer solution | pH: 7.5 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
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 FIELD |
Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K2 QUANTUM (4k x 4k) |
-Processing
EM software | Name: RELION / Version: 2 / Category: 3D reconstruction |
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CTF correction | Type: NONE |
3D reconstruction | Resolution: 4.57 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 40340 / Symmetry type: POINT |