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- PDB-7s5y: Human KATP channel in open conformation, focused on Kir and one S... -
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Open data
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Basic information
Entry | Database: PDB / ID: 7s5y | ||||||
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Title | Human KATP channel in open conformation, focused on Kir and one SUR, position 2 | ||||||
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![]() | MEMBRANE PROTEIN / ion channel / KATP / ATP-sensitive potassium channel | ||||||
Function / homology | ![]() negative regulation of neuroblast migration / positive regulation of uterine smooth muscle relaxation / ATP sensitive Potassium channels / Defective ABCC8 can cause hypo- and hyper-glycemias / positive regulation of tight junction disassembly / potassium ion-transporting ATPase complex / negative regulation of blood-brain barrier permeability / response to resveratrol / ATP-activated inward rectifier potassium channel activity / glutamate secretion, neurotransmission ...negative regulation of neuroblast migration / positive regulation of uterine smooth muscle relaxation / ATP sensitive Potassium channels / Defective ABCC8 can cause hypo- and hyper-glycemias / positive regulation of tight junction disassembly / potassium ion-transporting ATPase complex / negative regulation of blood-brain barrier permeability / response to resveratrol / ATP-activated inward rectifier potassium channel activity / glutamate secretion, neurotransmission / inward rectifying potassium channel / negative regulation of low-density lipoprotein particle clearance / cell body fiber / sulfonylurea receptor activity / ventricular cardiac muscle tissue development / CAMKK-AMPK signaling cascade / positive regulation of potassium ion transport / ATPase-coupled monoatomic cation transmembrane transporter activity / regulation of monoatomic ion transmembrane transport / response to pH / inorganic cation transmembrane transport / neuromuscular process / ankyrin binding / negative regulation of glial cell proliferation / response to ATP / : / response to zinc ion / response to testosterone / intracellular glucose homeostasis / potassium ion import across plasma membrane / action potential / positive regulation of insulin secretion involved in cellular response to glucose stimulus / potassium channel activity / intercalated disc / axolemma / ATPase-coupled transmembrane transporter activity / ABC-type transporter activity / negative regulation of insulin secretion / negative regulation of angiogenesis / potassium ion transmembrane transport / T-tubule / heat shock protein binding / positive regulation of protein localization to plasma membrane / potassium ion transport / acrosomal vesicle / response to ischemia / Regulation of insulin secretion / female pregnancy / determination of adult lifespan / cellular response to glucose stimulus / response to insulin / visual learning / sarcolemma / transmembrane transport / memory / ADP binding / synaptic vesicle membrane / cellular response to nicotine / nuclear envelope / positive regulation of tumor necrosis factor production / response to estradiol / cellular response to tumor necrosis factor / presynaptic membrane / transmembrane transporter binding / response to lipopolysaccharide / endosome / response to hypoxia / response to xenobiotic stimulus / neuronal cell body / glutamatergic synapse / apoptotic process / ATP hydrolysis activity / ATP binding / membrane / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.9 Å | ||||||
![]() | Zhao, C. / MacKinnon, R. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Molecular structure of an open human K channel. Authors: Chen Zhao / Roderick MacKinnon / ![]() Abstract: K channels are metabolic sensors that translate intracellular ATP/ADP balance into membrane excitability. The molecular composition of K includes an inward-rectifier potassium channel (Kir) and an ...K channels are metabolic sensors that translate intracellular ATP/ADP balance into membrane excitability. The molecular composition of K includes an inward-rectifier potassium channel (Kir) and an ABC transporter-like sulfonylurea receptor (SUR). Although structures of K have been determined in many conformations, in all cases, the pore in Kir is closed. Here, we describe human pancreatic K (hK) structures with an open pore at 3.1- to 4.0-Å resolution using single-particle cryo-electron microscopy (cryo-EM). Pore opening is associated with coordinated structural changes within the ATP-binding site and the channel gate in Kir. Conformational changes in SUR are also observed, resulting in an area reduction of contact surfaces between SUR and Kir. We also observe that pancreatic hK exhibits the unique (among inward-rectifier channels) property of PIP-independent opening, which appears to be correlated with a docked cytoplasmic domain in the absence of PIP. | ||||||
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Structure visualization
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Structure viewer | Molecule: ![]() ![]() |
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PDBx/mmCIF format | ![]() | 470.3 KB | Display | ![]() |
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PDB format | ![]() | 390.1 KB | Display | ![]() |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 24843MC ![]() 7s5tC ![]() 7s5vC ![]() 7s5xC ![]() 7s5zC ![]() 7s60C ![]() 7s61C C: citing same article ( M: map data used to model this data |
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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: 43622.746 Da / Num. of mol.: 4 / Mutation: C166S, G334D Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #2: Protein | | Mass: 177237.266 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #3: Chemical | ChemComp-ADP / | #4: Chemical | #5: Chemical | ChemComp-ATP / | Has ligand of interest | 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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Buffer solution | pH: 8.5 | ||||||||||||||||||||||||
Specimen | Conc.: 6.83 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||
Specimen support | Grid type: Quantifoil R1.2/1.3 | ||||||||||||||||||||||||
Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 289 K |
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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 / C2 aperture diameter: 100 µm |
Image recording | Electron dose: 57 e/Å2 / Detector mode: SUPER-RESOLUTION / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
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Processing
Software | Name: PHENIX / Version: 1.17.1_3660: / Classification: refinement | ||||||||||||||||||||||||
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
3D reconstruction | Resolution: 3.9 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 24689 / Symmetry type: POINT | ||||||||||||||||||||||||
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