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- PDB-6u9v: Cryo electron microscopy structure of the ATP-gated rat P2X7 ion ... -
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Basic information
Entry | Database: PDB / ID: 6u9v | |||||||||
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Title | Cryo electron microscopy structure of the ATP-gated rat P2X7 ion channel in the apo, closed state | |||||||||
![]() | P2X purinoceptor 7 | |||||||||
![]() | MEMBRANE PROTEIN / Ion Channel Apoptosis | |||||||||
Function / homology | ![]() The NLRP3 inflammasome / regulation of presynaptic dense core granule exocytosis / Platelet homeostasis / positive regulation of lymphocyte apoptotic process / positive regulation of bleb assembly / NAD transport / phagolysosome assembly / Elevation of cytosolic Ca2+ levels / phospholipid transfer to membrane / positive regulation of cytoskeleton organization ...The NLRP3 inflammasome / regulation of presynaptic dense core granule exocytosis / Platelet homeostasis / positive regulation of lymphocyte apoptotic process / positive regulation of bleb assembly / NAD transport / phagolysosome assembly / Elevation of cytosolic Ca2+ levels / phospholipid transfer to membrane / positive regulation of cytoskeleton organization / organic cation transport / purinergic nucleotide receptor activity / extracellularly ATP-gated monoatomic cation channel activity / lymphocyte apoptotic process / purinergic nucleotide receptor signaling pathway / gamma-aminobutyric acid secretion / positive regulation of monoatomic ion transmembrane transport / pore complex assembly / ATP export / positive regulation of interleukin-1 alpha production / negative regulation of cell volume / plasma membrane organization / cell death / positive regulation of gamma-aminobutyric acid secretion / : / collagen metabolic process / bleb / plasma membrane phospholipid scrambling / response to fluid shear stress / positive regulation of prostaglandin secretion / T cell apoptotic process / bleb assembly / ceramide biosynthetic process / mitochondrial depolarization / vesicle budding from membrane / programmed cell death / positive regulation of T cell apoptotic process / prostaglandin secretion / positive regulation of ossification / cellular response to dsRNA / glutamate secretion / cell volume homeostasis / positive regulation of glutamate secretion / negative regulation of bone resorption / positive regulation of macrophage cytokine production / skeletal system morphogenesis / phospholipid translocation / channel activity / nuclear inner membrane / negative regulation of MAPK cascade / response to ATP / positive regulation of catalytic activity / positive regulation of calcium ion transport into cytosol / positive regulation of mitochondrial depolarization / response to zinc ion / T cell homeostasis / synaptic vesicle exocytosis / monoatomic cation transport / membrane depolarization / membrane protein ectodomain proteolysis / cellular response to organic cyclic compound / neuronal action potential / protein secretion / positive regulation of bone mineralization / T cell proliferation / response to electrical stimulus / regulation of sodium ion transport / response to mechanical stimulus / extrinsic apoptotic signaling pathway / release of sequestered calcium ion into cytosol / homeostasis of number of cells within a tissue / sensory perception of pain / positive regulation of glycolytic process / reactive oxygen species metabolic process / protein serine/threonine kinase activator activity / : / mitochondrion organization / positive regulation of interleukin-1 beta production / positive regulation of cytokine production / establishment of localization in cell / positive regulation of protein secretion / lipopolysaccharide binding / apoptotic signaling pathway / response to bacterium / positive regulation of MAP kinase activity / neuromuscular junction / protein catabolic process / cell morphogenesis / terminal bouton / response to organic cyclic compound / T cell mediated cytotoxicity / protein processing / response to calcium ion / positive regulation of interleukin-6 production / positive regulation of T cell mediated cytotoxicity / calcium ion transport / MAPK cascade / cell-cell junction / presynapse / signaling receptor activity Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.9 Å | |||||||||
![]() | Mansoor, S.E. / McCarthy, A.E. | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Full-Length P2X Structures Reveal How Palmitoylation Prevents Channel Desensitization. Authors: Alanna E McCarthy / Craig Yoshioka / Steven E Mansoor / ![]() Abstract: P2X receptors are trimeric, non-selective cation channels activated by extracellular ATP. The P2X receptor subtype is a pharmacological target because of involvement in apoptotic, inflammatory, and ...P2X receptors are trimeric, non-selective cation channels activated by extracellular ATP. The P2X receptor subtype is a pharmacological target because of involvement in apoptotic, inflammatory, and tumor progression pathways. It is the most structurally and functionally distinct P2X subtype, containing a unique cytoplasmic domain critical for the receptor to initiate apoptosis and not undergo desensitization. However, lack of structural information about the cytoplasmic domain has hindered understanding of the molecular mechanisms underlying these processes. We report cryoelectron microscopy structures of full-length rat P2X receptor in apo and ATP-bound states. These structures reveal how one cytoplasmic element, the C-cys anchor, prevents desensitization by anchoring the pore-lining helix to the membrane with palmitoyl groups. They show a second cytoplasmic element with a unique fold, the cytoplasmic ballast, which unexpectedly contains a zinc ion complex and a guanosine nucleotide binding site. Our structures provide first insights into the architecture and function of a P2X receptor cytoplasmic domain. | |||||||||
History |
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Structure visualization
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Structure viewer | Molecule: ![]() ![]() |
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PDBx/mmCIF format | ![]() | 571.3 KB | Display | ![]() |
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PDB format | ![]() | 489.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 20702MC ![]() 6u9wC 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
-Protein , 1 types, 3 molecules ABC
#1: Protein | Mass: 69904.016 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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-Sugars , 3 types, 18 molecules ![](data/chem/img/NAG.gif)
#2: Polysaccharide | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source #3: Polysaccharide | #6: Sugar | ChemComp-NAG / |
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-Non-polymers , 4 types, 30 molecules ![](data/chem/img/GDP.gif)
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![](data/chem/img/Q3G.gif)
![](data/chem/img/PLM.gif)
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![](data/chem/img/Q3G.gif)
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#4: Chemical | #5: Chemical | ChemComp-ZN / #7: Chemical | #8: Chemical | ChemComp-PLM / |
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-Details
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
Component | Name: P2X7 receptor ion channel / Type: COMPLEX / Entity ID: #1 / Source: RECOMBINANT |
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Molecular weight | Experimental value: NO |
Source (natural) | Organism: ![]() ![]() |
Source (recombinant) | Organism: ![]() |
Buffer solution | pH: 7 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Specimen support | Details: unspecified |
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: 27 e/Å2 / Film or detector model: FEI FALCON III (4k x 4k) |
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Processing
CTF correction | Type: PHASE FLIPPING ONLY |
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3D reconstruction | Resolution: 2.9 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 77697 / Symmetry type: POINT |