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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-9389 | |||||||||
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Title | Architecture and subunit arrangement of native AMPA receptors | |||||||||
![]() | Complex | |||||||||
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Function / homology | ![]() Presynaptic depolarization and calcium channel opening / Cargo concentration in the ER / cellular response to amine stimulus / axonal spine / COPII-mediated vesicle transport / positive regulation of membrane potential / eye blink reflex / positive regulation of protein localization to basolateral plasma membrane / chemical synaptic transmission, postsynaptic / cellular response to ammonium ion ...Presynaptic depolarization and calcium channel opening / Cargo concentration in the ER / cellular response to amine stimulus / axonal spine / COPII-mediated vesicle transport / positive regulation of membrane potential / eye blink reflex / positive regulation of protein localization to basolateral plasma membrane / chemical synaptic transmission, postsynaptic / cellular response to ammonium ion / cerebellar mossy fiber / neurotransmitter receptor transport, postsynaptic endosome to lysosome / LGI-ADAM interactions / myosin V binding / neurotransmitter receptor activity involved in regulation of postsynaptic cytosolic calcium ion concentration / Trafficking of AMPA receptors / neuron spine / regulation of AMPA receptor activity / neurotransmitter receptor internalization / response to arsenic-containing substance / membrane hyperpolarization / cellular response to dsRNA / postsynaptic neurotransmitter receptor diffusion trapping / nervous system process / dendritic spine membrane / Synaptic adhesion-like molecules / protein targeting to membrane / long-term synaptic depression / parallel fiber to Purkinje cell synapse / beta-2 adrenergic receptor binding / cellular response to peptide hormone stimulus / voltage-gated calcium channel complex / protein heterotetramerization / neurotransmitter receptor localization to postsynaptic specialization membrane / protein kinase A binding / neuromuscular junction development / spinal cord development / spine synapse / dendritic spine neck / neuronal cell body membrane / dendritic spine head / Activation of AMPA receptors / perisynaptic space / transmission of nerve impulse / AMPA glutamate receptor activity / channel regulator activity / ligand-gated monoatomic cation channel activity / Trafficking of GluR2-containing AMPA receptors / response to lithium ion / regulation of postsynaptic membrane neurotransmitter receptor levels / immunoglobulin binding / membrane depolarization / AMPA glutamate receptor complex / adenylate cyclase binding / kainate selective glutamate receptor activity / cellular response to organic cyclic compound / ionotropic glutamate receptor complex / excitatory synapse / extracellularly glutamate-gated ion channel activity / neuronal action potential / cellular response to glycine / calcium channel regulator activity / asymmetric synapse / G-protein alpha-subunit binding / regulation of receptor recycling / voltage-gated calcium channel activity / regulation of postsynaptic membrane potential / Unblocking of NMDA receptors, glutamate binding and activation / postsynaptic density, intracellular component / positive regulation of synaptic transmission / glutamate receptor binding / long-term memory / extracellular ligand-gated monoatomic ion channel activity / positive regulation of synaptic transmission, glutamatergic / synaptic cleft / response to electrical stimulus / glutamate-gated receptor activity / glutamate-gated calcium ion channel activity / presynaptic active zone membrane / response to fungicide / monoatomic ion transmembrane transport / regulation of synaptic transmission, glutamatergic / somatodendritic compartment / synapse assembly / cellular response to brain-derived neurotrophic factor stimulus / dendrite membrane / ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential / cytoskeletal protein binding / ionotropic glutamate receptor binding / dendrite cytoplasm / ionotropic glutamate receptor signaling pathway / hippocampal mossy fiber to CA3 synapse / cellular response to amino acid stimulus / regulation of membrane potential / SNARE binding / response to cocaine / transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential / dendritic shaft / synaptic membrane / synaptic transmission, glutamatergic Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() ![]() ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 6.5 Å | |||||||||
![]() | Gouaux E / Zhao Y | |||||||||
![]() | ![]() Title: Architecture and subunit arrangement of native AMPA receptors elucidated by cryo-EM. Authors: Yan Zhao / Shanshuang Chen / Adam C Swensen / Wei-Jun Qian / Eric Gouaux / ![]() Abstract: Glutamate-gated AMPA receptors mediate the fast component of excitatory signal transduction at chemical synapses throughout all regions of the mammalian brain. AMPA receptors are tetrameric ...Glutamate-gated AMPA receptors mediate the fast component of excitatory signal transduction at chemical synapses throughout all regions of the mammalian brain. AMPA receptors are tetrameric assemblies composed of four subunits, GluA1-GluA4. Despite decades of study, the subunit composition, subunit arrangement, and molecular structure of native AMPA receptors remain unknown. Here we elucidate the structures of 10 distinct native AMPA receptor complexes by single-particle cryo-electron microscopy (cryo-EM). We find that receptor subunits are arranged nonstochastically, with the GluA2 subunit preferentially occupying the B and D positions of the tetramer and with triheteromeric assemblies comprising a major population of native AMPA receptors. Cryo-EM maps define the structure for S2-M4 linkers between the ligand-binding and transmembrane domains, suggesting how neurotransmitter binding is coupled to ion channel gating. | |||||||||
History |
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Structure visualization
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 8.4 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 33.1 KB 33.1 KB | Display Display | ![]() |
Images | ![]() | 113.6 KB | ||
Others | ![]() ![]() ![]() | 6.4 MB 7.7 MB 8.6 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6njnMC ![]() 0426C ![]() 0427C ![]() 0428C ![]() 0429C ![]() 0430C ![]() 0431C ![]() 0432C ![]() 9387C ![]() 9388C ![]() 6njlC ![]() 6njmC M: atomic model generated by this map C: citing same article ( |
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Similar structure data |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Annotation | Complex | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.72 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Additional map: Complex
File | emd_9389_additional_1.map | ||||||||||||
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Annotation | Complex | ||||||||||||
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-Additional map: Complex
File | emd_9389_additional_2.map | ||||||||||||
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Annotation | Complex | ||||||||||||
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-Additional map: Complex
File | emd_9389_additional_3.map | ||||||||||||
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Annotation | Complex | ||||||||||||
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Density Histograms |
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Sample components
+Entire : Native GluA1/GluA2/GluA3/GluA2 complex bound with MPQX
+Supramolecule #1: Native GluA1/GluA2/GluA3/GluA2 complex bound with MPQX
+Supramolecule #2: ATD-LBD layers of native tri-heteromeric A1A2A3A2 AMPAR
+Supramolecule #3: LBD-TMD layers of native tri-heteromeric A1A2A3A2 AMPAR
+Supramolecule #4: ATD layer of native tri-heteromeric A1A2A3A2 AMPAR
+Macromolecule #1: Glutamate receptor 1
+Macromolecule #2: Glutamate receptor 2
+Macromolecule #3: Glutamate receptor 3
+Macromolecule #4: A'-C' auxiliary proteins
+Macromolecule #5: Voltage-dependent calcium channel gamma-2 subunit
+Macromolecule #6: 11B8 scFv
+Macromolecule #7: 15F1 Fab light chain
+Macromolecule #8: 15F1 Fab heavy chain
+Macromolecule #9: 5B2 Fab
+Macromolecule #12: {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquino...
+Macromolecule #13: 2-acetamido-2-deoxy-beta-D-glucopyranose
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Concentration | 4 mg/mL | ||||||||||||
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Buffer | pH: 8 Component:
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Grid | Details: unspecified | ||||||||||||
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 295 K |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: SUPER-RESOLUTION / Average electron dose: 54.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 6.5 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION / Number images used: 161000 |
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Initial angle assignment | Type: RANDOM ASSIGNMENT |
Final angle assignment | Type: RANDOM ASSIGNMENT |
Final 3D classification | Number classes: 10 |
-Atomic model buiding 1
Refinement | Space: REAL / Protocol: RIGID BODY FIT |
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Output model | ![]() PDB-6njn: |