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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 / regulation of respiratory gaseous exchange / serotonin metabolic process / regulation of ARF protein signal transduction / response to manganese ion / transmitter-gated monoatomic ion channel activity / suckling behavior / positive regulation of inhibitory postsynaptic potential / sleep / cellular response to dsRNA / response to carbohydrate / propylene metabolic process / response to glycine / cellular response to lipid / regulation of NMDA receptor activity / dendritic spine organization / RAF/MAP kinase cascade / locomotion / response to amine / neurotransmitter receptor complex / Synaptic adhesion-like molecules / response to glycoside / 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 / response to morphine / regulation of dendrite morphogenesis / protein heterotetramerization / male mating behavior / regulation of synapse assembly / spinal cord development / glycine binding / startle response / positive regulation of reactive oxygen species biosynthetic process / cellular response to zinc ion / parallel fiber to Purkinje cell synapse / response to lithium ion / dopamine metabolic process / monoatomic ion channel complex / monoatomic cation transmembrane transport / regulation of postsynaptic membrane potential / action potential / positive regulation of calcium ion transport into cytosol / cellular response to glycine / modulation of excitatory postsynaptic potential / associative learning / positive regulation of dendritic spine maintenance / response to light stimulus / regulation of neuronal synaptic plasticity / social behavior / Unblocking of NMDA receptors, glutamate binding and activation / positive regulation of protein targeting to membrane / conditioned place preference / monoatomic cation transport / glutamate receptor binding / prepulse inhibition / ligand-gated monoatomic ion channel activity / neuron development / multicellular organismal response to stress / long-term memory / phosphatase binding / postsynaptic density, intracellular component / response to fungicide / monoatomic cation channel activity / synaptic cleft / calcium ion homeostasis / positive regulation of synaptic transmission, glutamatergic / glutamate-gated receptor activity / cellular response to manganese ion / glutamate-gated calcium ion channel activity / presynaptic active zone membrane / excitatory synapse / cell adhesion molecule binding / dendrite membrane 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
