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Yorodumi- EMDB-45279: Diheteromeric GluN1/GluN2A (delM653) in nanodisc complexed with g... -
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Open data
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Basic information
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| Title | Diheteromeric GluN1/GluN2A (delM653) in nanodisc complexed with glycine, glutamate, and GNE-4123, open conformation | |||||||||
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Keywords | ion channel / NMDA / positive allosteric modulator / open pore conformation / TRANSPORT PROTEIN | |||||||||
| Function / homology | Function and homology informationregulation of response to alcohol / response to ammonium ion / neurotransmitter receptor transport, plasma membrane to endosome / receptor recycling / response to environmental enrichment / directional locomotion / pons maturation / EPHB-mediated forward signaling / Assembly and cell surface presentation of NMDA receptors / regulation of cell communication ...regulation of response to alcohol / response to ammonium ion / neurotransmitter receptor transport, plasma membrane to endosome / receptor recycling / response to environmental enrichment / directional locomotion / pons maturation / EPHB-mediated forward signaling / Assembly and cell surface presentation of NMDA receptors / regulation of cell communication / auditory behavior / positive regulation of Schwann cell migration / olfactory learning / response to other organism / response to hydrogen sulfide / cellular response to magnesium ion / dendritic branch / conditioned taste aversion / response to methylmercury / protein localization to postsynaptic membrane / serotonin metabolic process / regulation of ARF protein signal transduction / regulation of respiratory gaseous exchange / response to manganese ion / transmitter-gated monoatomic ion channel activity / suckling behavior / sleep / positive regulation of inhibitory postsynaptic potential / response to carbohydrate / cellular response to lipid / propylene metabolic process / response to glycine / regulation of NMDA receptor activity / cellular response to dsRNA / dendritic spine organization / RAF/MAP kinase cascade / locomotion / response to amine / neurotransmitter receptor complex / response to glycoside / Synaptic adhesion-like molecules / regulation of monoatomic cation transmembrane transport / NMDA glutamate receptor activity / voltage-gated monoatomic cation channel activity / NMDA selective glutamate receptor complex / glutamate binding / ligand-gated sodium channel activity / glutamate receptor signaling pathway / neuromuscular process / regulation of axonogenesis / calcium ion transmembrane import into cytosol / regulation of dendrite morphogenesis / male mating behavior / regulation of synapse assembly / protein heterotetramerization / response to morphine / spinal cord development / glycine binding / startle response / positive regulation of reactive oxygen species biosynthetic process / dopamine metabolic process / cellular response to zinc ion / parallel fiber to Purkinje cell synapse / response to lithium ion / monoatomic ion channel complex / regulation of postsynaptic membrane potential / monoatomic cation transmembrane transport / action potential / positive regulation of calcium ion transport into cytosol / cellular response to glycine / associative learning / positive regulation of dendritic spine maintenance / modulation of excitatory postsynaptic potential / response to light stimulus / Unblocking of NMDA receptors, glutamate binding and activation / regulation of neuronal synaptic plasticity / positive regulation of protein targeting to membrane / monoatomic cation transport / prepulse inhibition / glutamate receptor binding / conditioned place preference / social behavior / ligand-gated monoatomic ion channel activity / multicellular organismal response to stress / neuron development / phosphatase binding / long-term memory / postsynaptic density, intracellular component / monoatomic cation channel activity / synaptic cleft / response to fungicide / calcium ion homeostasis / positive regulation of synaptic transmission, glutamatergic / cellular response to manganese ion / glutamate-gated receptor activity / glutamate-gated calcium ion channel activity / presynaptic active zone membrane / cell adhesion molecule binding / sensory perception of pain / excitatory synapse Similarity search - Function | |||||||||
| Biological species | ![]() ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.1 Å | |||||||||
Authors | Jalali-Yazdi F / Kim J / Gouaux E | |||||||||
| Funding support | United States, 1 items
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Citation | Journal: Sci Adv / Year: 2025Title: Cryo-EM snapshots of NMDA receptor activation illuminate sequential rearrangements. Authors: Jamie A Abbott / Junhoe Kim / Beiying Liu / Gabriela K Popescu / Eric Gouaux / Farzad Jalali-Yazdi / ![]() Abstract: Canonical -methyl-d-aspartate receptors (NMDARs) are glutamate-gated ion channels with critical roles in the development and function of the nervous system. The excitatory currents they produce ...Canonical -methyl-d-aspartate receptors (NMDARs) are glutamate-gated ion channels with critical roles in the development and function of the nervous system. The excitatory currents they produce reflect stochastic transitions between multiple agonist-bound closed- and open-pore states. We leveraged the intrinsically high open probability () of NMDARs composed of GluN1 and GluN2A subunits, together with judiciously chosen mutants and ligands, to achieve conditions in which receptors had a near unity. Using single-particle cryo-electron microscopy (cryo-EM), we captured three activated receptor states, each with distinct conformations of the gate-forming M3 helices. Separately, we carried out single-channel electrophysiology, together with statistical modeling, to relate the cryo-EM structures to the gating reaction. NMDAR channel opening involves bending of the pore-forming M3 helices to produce a transient open-channel conformation, subsequently stabilized by new interactions between the D2-M3 linkers with the pre-M1 helices and the pre-M4 loops, to yield the stable open channel. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_45279.map.gz | 95.7 MB | EMDB map data format | |
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| Header (meta data) | emd-45279-v30.xml emd-45279.xml | 28.8 KB 28.8 KB | Display Display | EMDB header |
| Images | emd_45279.png | 141.9 KB | ||
| Filedesc metadata | emd-45279.cif.gz | 8.4 KB | ||
| Others | emd_45279_additional_1.map.gz emd_45279_half_map_1.map.gz emd_45279_half_map_2.map.gz | 95.7 MB 475.6 MB 475.6 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-45279 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-45279 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9c7cMC ![]() 9c7eMC ![]() 9c7pC ![]() 9c7qC ![]() 9c7rC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_45279.map.gz / Format: CCP4 / Size: 103 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.826 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Additional map: A map processed in C2 symmetry
| File | emd_45279_additional_1.map | ||||||||||||
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| Annotation | A map processed in C2 symmetry | ||||||||||||
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-Half map: #2
| File | emd_45279_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #1
| File | emd_45279_half_map_2.map | ||||||||||||
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Sample components
+Entire : Diheteromeric NMDA receptor GluN1/GluN2A in nanodisc, in complex ...
+Supramolecule #1: Diheteromeric NMDA receptor GluN1/GluN2A in nanodisc, in complex ...
+Macromolecule #1: Glutamate receptor ionotropic, NMDA 1,Green fluorescent protein
+Macromolecule #2: Glutamate receptor ionotropic, NMDA 2A,Green fluorescent protein ...
+Macromolecule #4: 4-cyclohexyl-N-[(8R)-2-cyclopropyl-7-hydroxy-5-methyl[1,2,4]triaz...
+Macromolecule #5: 2-acetamido-2-deoxy-beta-D-glucopyranose
+Macromolecule #6: HEPTANE
+Macromolecule #7: CHOLESTEROL HEMISUCCINATE
+Macromolecule #8: GLYCINE
+Macromolecule #9: DODECANE
+Macromolecule #10: GLUTAMIC ACID
+Macromolecule #11: DECANE
+Macromolecule #12: HEXANE
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Concentration | 2 mg/mL |
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| Buffer | pH: 9 |
| Grid | Model: Quantifoil R2/1 / Material: GOLD / Mesh: 300 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 60 sec. / Details: 15 mA |
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 291 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Image recording | Film or detector model: GATAN K2 QUANTUM (4k x 4k) / Detector mode: COUNTING / Number real images: 8048 / Average exposure time: 1.8 sec. / Average electron dose: 53.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.8 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
| Refinement | Space: REAL / Protocol: RIGID BODY FIT / Target criteria: Cross-correlation coefficient |
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| Output model | ![]() PDB-9c7c: ![]() PDB-9c7e: |
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About Yorodumi



Keywords

Authors
United States, 1 items
Citation













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Homo sapiens (human)







FIELD EMISSION GUN
