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- EMDB-33791: Structure of the Rat tri-heteromeric GluN1-GluN2A-GluN2C NMDA rec... -

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Entry
Database: EMDB / ID: EMD-33791
TitleStructure of the Rat tri-heteromeric GluN1-GluN2A-GluN2C NMDA receptor in complex with glycine and glutamate
Map data
Sample
  • Organelle or cellular component: Rat tri-heteromeric GluN1-GluN2A-GluN2C NMDA receptor in complex with glycine and glutamate
    • Protein or peptide: Glutamate receptor ionotropic, NMDA 1
    • Protein or peptide: Glutamate receptor
    • Protein or peptide: Glutamate receptor ionotropic, NMDA 2C
  • Ligand: 2-acetamido-2-deoxy-beta-D-glucopyranose
  • Ligand: GLYCINE
  • Ligand: GLUTAMIC ACID
KeywordsNMDA receptor / GluN2C / GluN2A / MEMBRANE PROTEIN
Function / homology
Function and homology information


directional locomotion / pons maturation / positive regulation of Schwann cell migration / regulation of cell communication / EPHB-mediated forward signaling / Assembly and cell surface presentation of NMDA receptors / olfactory learning / conditioned taste aversion / dendritic branch / regulation of respiratory gaseous exchange ...directional locomotion / pons maturation / positive regulation of Schwann cell migration / regulation of cell communication / EPHB-mediated forward signaling / Assembly and cell surface presentation of NMDA receptors / olfactory learning / conditioned taste aversion / dendritic branch / regulation of respiratory gaseous exchange / serotonin metabolic process / protein localization to postsynaptic membrane / transmitter-gated monoatomic ion channel activity / suckling behavior / sleep / response to glycine / propylene metabolic process / regulation of monoatomic cation transmembrane transport / NMDA glutamate receptor activity / Synaptic adhesion-like molecules / RAF/MAP kinase cascade / voltage-gated monoatomic cation channel activity / response to glycoside / NMDA selective glutamate receptor complex / neurotransmitter receptor complex / ligand-gated sodium channel activity / glutamate binding / response to morphine / neuromuscular process controlling balance / calcium ion transmembrane import into cytosol / regulation of axonogenesis / neuromuscular process / regulation of dendrite morphogenesis / protein heterotetramerization / male mating behavior / glycine binding / regulation of synapse assembly / response to amine / parallel fiber to Purkinje cell synapse / startle response / positive regulation of reactive oxygen species biosynthetic process / monoatomic cation transmembrane transport / dopamine metabolic process / positive regulation of calcium ion transport into cytosol / regulation of neuron apoptotic process / associative learning / cellular response to glycine / monoatomic cation transport / excitatory synapse / social behavior / positive regulation of dendritic spine maintenance / regulation of neuronal synaptic plasticity / monoatomic ion channel complex / positive regulation of excitatory postsynaptic potential / glutamate receptor binding / Unblocking of NMDA receptors, glutamate binding and activation / long-term memory / positive regulation of synaptic transmission, glutamatergic / synaptic cleft / prepulse inhibition / phosphatase binding / monoatomic cation channel activity / calcium ion homeostasis / response to fungicide / glutamate-gated receptor activity / glutamate-gated calcium ion channel activity / cellular response to manganese ion / presynaptic active zone membrane / neurogenesis / sensory perception of pain / dendrite membrane / ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential / sodium ion transmembrane transport / ionotropic glutamate receptor signaling pathway / synaptic membrane / hippocampal mossy fiber to CA3 synapse / response to amphetamine / adult locomotory behavior / excitatory postsynaptic potential / regulation of membrane potential / learning / transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential / synaptic transmission, glutamatergic / PDZ domain binding / protein catabolic process / regulation of long-term neuronal synaptic plasticity / response to calcium ion / postsynaptic density membrane / negative regulation of protein catabolic process / neuron cellular homeostasis / calcium ion transmembrane transport / visual learning / regulation of synaptic plasticity / cerebral cortex development / calcium channel activity / response to wounding / memory / long-term synaptic potentiation / intracellular calcium ion homeostasis / terminal bouton
Similarity search - Function
Glutamate [NMDA] receptor, epsilon subunit, C-terminal / N-methyl D-aspartate receptor 2B3 C-terminus / : / : / Ionotropic glutamate receptor, metazoa / Ligated ion channel L-glutamate- and glycine-binding site / Ionotropic glutamate receptor, L-glutamate and glycine-binding domain / Ligated ion channel L-glutamate- and glycine-binding site / Ligand-gated ion channel / : ...Glutamate [NMDA] receptor, epsilon subunit, C-terminal / N-methyl D-aspartate receptor 2B3 C-terminus / : / : / Ionotropic glutamate receptor, metazoa / Ligated ion channel L-glutamate- and glycine-binding site / Ionotropic glutamate receptor, L-glutamate and glycine-binding domain / Ligated ion channel L-glutamate- and glycine-binding site / Ligand-gated ion channel / : / Ionotropic glutamate receptor / Eukaryotic homologues of bacterial periplasmic substrate binding proteins. / Receptor, ligand binding region / Receptor family ligand binding region / Periplasmic binding protein-like I
Similarity search - Domain/homology
Glutamate receptor / Glutamate receptor ionotropic, NMDA 1 / Glutamate receptor ionotropic, NMDA 2C
Similarity search - Component
Biological speciesRattus norvegicus (Norway rat)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.3 Å
AuthorsZhang M / Zhang J / Guo F / Li Y / Zhu S
Funding support China, 1 items
OrganizationGrant numberCountry
Chinese Academy of Sciences China
Citation
Journal: Nat Struct Mol Biol / Year: 2023
Title: Distinct structure and gating mechanism in diverse NMDA receptors with GluN2C and GluN2D subunits.
Authors: Jilin Zhang / Ming Zhang / Qinrui Wang / Han Wen / Zheyi Liu / Fangjun Wang / Yuhang Wang / Fenyong Yao / Nan Song / Zengwei Kou / Yang Li / Fei Guo / Shujia Zhu /
Abstract: N-methyl-D-aspartate (NMDA) receptors are heterotetramers comprising two GluN1 and two alternate GluN2 (N2A-N2D) subunits. Here we report full-length cryo-EM structures of the human N1-N2D di- ...N-methyl-D-aspartate (NMDA) receptors are heterotetramers comprising two GluN1 and two alternate GluN2 (N2A-N2D) subunits. Here we report full-length cryo-EM structures of the human N1-N2D di-heterotetramer (di-receptor), rat N1-N2C di-receptor and N1-N2A-N2C tri-heterotetramer (tri-receptor) at a best resolution of 3.0 Å. The bilobate N-terminal domain (NTD) in N2D intrinsically adopts a closed conformation, leading to a compact NTD tetramer in the N1-N2D receptor. Additionally, crosslinking the ligand-binding domain (LBD) of two N1 protomers significantly elevated the channel open probability (Po) in N1-N2D di-receptors. Surprisingly, the N1-N2C di-receptor adopted both symmetric (minor) and asymmetric (major) conformations, the latter further locked by an allosteric potentiator, PYD-106, binding to a pocket between the NTD and LBD in only one N2C protomer. Finally, the N2A and N2C subunits in the N1-N2A-N2C tri-receptor display a conformation close to one protomer in the N1-N2A and N1-N2C di-receptors, respectively. These findings provide a comprehensive structural understanding of diverse function in major NMDA receptor subtypes.
#1: Journal: Nat.Struct.Mol.Biol. / Year: 2023
Title: Distinct structure and gating mechanism in diverse NMDA receptors with GluN2C and GluN2D subunits
Authors: Zhang M / Zhu S
History
DepositionJul 8, 2022-
Header (metadata) releaseMar 29, 2023-
Map releaseMar 29, 2023-
UpdateOct 23, 2024-
Current statusOct 23, 2024Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_33791.png

Downloads & links

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Map

FileDownload / File: emd_33791.map.gz / Format: CCP4 / Size: 93 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

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AxesZ (Sec.)Y (Row.)X (Col.)
1.07 Å/pix.
x 290 pix.
= 310.59 Å		1.07 Å/pix.
x 290 pix.
= 310.59 Å		1.07 Å/pix.
x 290 pix.
= 310.59 Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.071 Å
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Histogram (log scale)
Contour LevelBy AUTHOR: 0.018
Minimum - Maximum-0.032320492 - 0.09014163
Average (Standard dev.)0.00038191627 (±0.0027805169)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions290290290
Spacing290290290
CellA=B=C: 310.59 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #2

Fileemd_33791_half_map_1.map
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Half map: #1

Fileemd_33791_half_map_2.map
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Sample components

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Entire : Rat tri-heteromeric GluN1-GluN2A-GluN2C NMDA receptor in complex ...

EntireName: Rat tri-heteromeric GluN1-GluN2A-GluN2C NMDA receptor in complex with glycine and glutamate
Components
  • Organelle or cellular component: Rat tri-heteromeric GluN1-GluN2A-GluN2C NMDA receptor in complex with glycine and glutamate
    • Protein or peptide: Glutamate receptor ionotropic, NMDA 1
    • Protein or peptide: Glutamate receptor
    • Protein or peptide: Glutamate receptor ionotropic, NMDA 2C
  • Ligand: 2-acetamido-2-deoxy-beta-D-glucopyranose
  • Ligand: GLYCINE
  • Ligand: GLUTAMIC ACID

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Supramolecule #1: Rat tri-heteromeric GluN1-GluN2A-GluN2C NMDA receptor in complex ...

SupramoleculeName: Rat tri-heteromeric GluN1-GluN2A-GluN2C NMDA receptor in complex with glycine and glutamate
type: organelle_or_cellular_component / ID: 1 / Parent: 0 / Macromolecule list: #1-#3
Source (natural)Organism: Rattus norvegicus (Norway rat)

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Macromolecule #1: Glutamate receptor ionotropic, NMDA 1

MacromoleculeName: Glutamate receptor ionotropic, NMDA 1 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Rattus norvegicus (Norway rat)
Molecular weightTheoretical: 89.956797 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MSTMHLLTFA LLFSCSFARA ACDPKIVNIG AVLSTRKHEQ MFREAVNQAN KRHGSWKIQL NATSVTHKPN AIQMALSVCE DLISSQVYA ILVSHPPTPN DHFTPTPVSY TAGFYRIPVL GLTTRMSIYS DKSIHLSFLR TVPPYSHQSS VWFEMMRVYN W NHIILLVS ...String:
MSTMHLLTFA LLFSCSFARA ACDPKIVNIG AVLSTRKHEQ MFREAVNQAN KRHGSWKIQL NATSVTHKPN AIQMALSVCE DLISSQVYA ILVSHPPTPN DHFTPTPVSY TAGFYRIPVL GLTTRMSIYS DKSIHLSFLR TVPPYSHQSS VWFEMMRVYN W NHIILLVS DDHEGRAAQK RLETLLEERE SKAEKVLQFD PGTKNVTALL MEARELEARV IILSASEDDA ATVYRAAAML NM TGSGYVW LVGEREISGN ALRYAPDGII GLQLINGKNE SAHISDAVGV VAQAVHELLE KENITDPPRG CVGNTNIWKT GPL FKRVLM SSKYADGVTG RVEFNEDGDR KFANYSIMNL QNRKLVQVGI YNGTHVIPND RKIIWPGGET EKPRGYQMST RLKI VTIHQ EPFVYVKPTM SDGTCKEEFT VNGDPVKKVI CTGPNDTSPG SPRHTVPQCC YGFCIDLLIK LARTMNFTYE VHLVA DGKF GTQERVNNSN KKEWNGMMGE LLSGQADMIV APLTINNERA QYIEFSKPFK YQGLTILVKK EIPRSTLDSF MQPFQS TLW LLVGLSVHVV AVMLYLLDRF SPFGRFKVNS EEEEEDALTL SSAMWFSWGV LLNSGIGEGA PRSFSARILG MVWAGFA MI IVASYTANLA AFLVLDRPEE RITGINDPRL RNPSDKFIYA TVKQSSVDIY FRRQVELSTM YRHMEKHNYE SAAEAIQA V RDNKLHAFIW DSAVLEFEAS QKCDLVTTGE LFFRSGFGIG MRKDSPWKQN VSLSILKSHE NGFMEDLDKT WVRYQEC

UniProtKB: Glutamate receptor ionotropic, NMDA 1

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Macromolecule #2: Glutamate receptor

MacromoleculeName: Glutamate receptor / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Rattus norvegicus (Norway rat)
Molecular weightTheoretical: 93.837469 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: PMGRLGYWTL LVLPALLVWR DPAQNAAAEK GPPALNIAVL LGHSHDVTER ELRNLWGPEQ ATGLPLDVNV VALLMNRTDP KSLITHVCD LMSGARIHGL VFGDDTDQEA VAQMLDFISS QTFIPILGIH GGASMIMADK DPTSTFFQFG ASIQQQATVM L KIMQDYDW ...String:
PMGRLGYWTL LVLPALLVWR DPAQNAAAEK GPPALNIAVL LGHSHDVTER ELRNLWGPEQ ATGLPLDVNV VALLMNRTDP KSLITHVCD LMSGARIHGL VFGDDTDQEA VAQMLDFISS QTFIPILGIH GGASMIMADK DPTSTFFQFG ASIQQQATVM L KIMQDYDW HVFSLVTTIF PGYRDFISFI KTTVDNSFVG WDMQNVITLD TSFEDAKTQV QLKKIHSSVI LLYCSKDEAV LI LSEARSL GLTGYDFFWI VPSLVSGNTE LIPKEFPSGL ISVSYDDWDY SLEARVRDGL GILTTAASSM LEKFSYIPEA KAS CYGQAE KPETPLHTLH QFMVNVTWDG KDLSFTEEGY QVHPRLVVIV LNKDREWEKV GKWENQTLSL RHAVWPRYKS FSDC EPDDN HLSIVTLEEA PFVIVEDIDP LTETCVRNTV PCRKFVKINN STNEGMNVKK CCKGFCIDIL KKLSRTVKFT YDLYL VTNG KHGKKVNNVW NGMIGEVVYQ RAVMAVGSLT INEERSEVVD FSVPFVETGI SVMVSRSNGT VSPSAFLEPF SASVWV MMF VMLLIVSAIA VFVFEYFSPV GYNRNLAKGK APHGPSFTIG KAIWLLWGLV FNNSVPVQNP KGTTSKIMVS VWAFFAV IF LASYTANLAA FMIQEEFVDQ VTGLSDKKFQ RPHDYSPPFR FGTVPNGSTE RNIRNNYPYM HQYMTRFNQR GVEDALVS L KTGKLDAFIY DAAVLNYKAG RDEGCKLVTI GSGYIFATTG YGIALQKGSP WKRQIDLALL QFVGDGEMEE LETLWLTGI CHNEKNEVMS SQLDIDNMAG VFYMLAAAMA LSLITFIW

UniProtKB: Glutamate receptor

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Macromolecule #3: Glutamate receptor ionotropic, NMDA 2C

MacromoleculeName: Glutamate receptor ionotropic, NMDA 2C / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Rattus norvegicus (Norway rat)
Molecular weightTheoretical: 91.658445 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MGGALGPALL LTSLLGAWAR LGAGQGEQAV TVAVVFGSSG PLQTQARTRL TSQNFLDLPL EIQPLTVGVN NTNPSSILTQ ICGLLGAAR VHGIVFEDNV DTEAVAQLLD FVSSQTHVPI LSISGGSAVV LTPKEPGSAF LQLGVSLEQQ LQVLFKVLEE Y DWSAFAVI ...String:
MGGALGPALL LTSLLGAWAR LGAGQGEQAV TVAVVFGSSG PLQTQARTRL TSQNFLDLPL EIQPLTVGVN NTNPSSILTQ ICGLLGAAR VHGIVFEDNV DTEAVAQLLD FVSSQTHVPI LSISGGSAVV LTPKEPGSAF LQLGVSLEQQ LQVLFKVLEE Y DWSAFAVI TSLHPGHALF LEGVRAVADA SYLSWRLLDV LTLELGPGGP RARTQRLLRQ VDAPVLVAYC SREEAEVLFA EA AQAGLVG PGHVWLVPNL ALGSTDAPPA AFPVGLISVV TESWRLSLRQ KVRDGVAILA LGAHSYRRQY GTLPAPAGDC RSH PGPVSP AREAFYRHLL NVTWEGRDFS FSPGGYLVRP TMVVIALNRH RLWEMVGRWD HGVLYMKYPV WPRYSTSLQP VVDS RHLTV ATLEERPFVI VESPDPGTGG CVPNTVPCRR QSNHTFSSGD LTPYTKLCCK GFCIDILKKL AKVVKFSYDL YLVTN GKHG KRVRGVWNGM IGEVYYKRAD MAIGSLTINE ERSEIIDFSV PFVETGISVM VSRSNGTVSP SAFLEPYSPA VWVMMF VMC LTVVAITVFM FEYFSPVSYN QNLTKGKKPG GPSFTIGKSV WLLWALVFNN SVPIENPRGT TSKIMVLVWA FFAVIFL AS YTANLAAFMI QEQYIDTVSG LSDKKFQRPQ DQYPPFRFGT VPNGSTERNI RSNYRDMHTH MVKFNQRSVE DALTSLKM G KLDAFIYDAA VLNYMAGKDE GCKLVTIGSG KVFATTGYGI AMQKDSHWKR AIDLALLQLL GDGETQKLET VWLSGICQN EKNEVMSSKL DIDNMAGVFY MLLVAMGLAL LVFAW

UniProtKB: Glutamate receptor ionotropic, NMDA 2C

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Macromolecule #6: 2-acetamido-2-deoxy-beta-D-glucopyranose

MacromoleculeName: 2-acetamido-2-deoxy-beta-D-glucopyranose / type: ligand / ID: 6 / Number of copies: 21 / Formula: NAG
Molecular weightTheoretical: 221.208 Da
Chemical component information

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

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Macromolecule #7: GLYCINE

MacromoleculeName: GLYCINE / type: ligand / ID: 7 / Number of copies: 2 / Formula: GLY
Molecular weightTheoretical: 75.067 Da
Chemical component information

ChemComp-GLY:
GLYCINE

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Macromolecule #8: GLUTAMIC ACID

MacromoleculeName: GLUTAMIC ACID / type: ligand / ID: 8 / Number of copies: 2 / Formula: GLU
Molecular weightTheoretical: 147.129 Da
Chemical component information

ChemComp-GLU:
GLUTAMIC ACID

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

Concentration4.2 mg/mL
BufferpH: 8
GridModel: Quantifoil R1.2/1.3 / Material: GOLD / Mesh: 300 / Pretreatment - Type: GLOW DISCHARGE
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 281 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: DIRECT ELECTRON DE-10 (5k x 4k) / Digitization - Dimensions - Width: 5760 pixel / Digitization - Dimensions - Height: 9042 pixel / Average electron dose: 60.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.2 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 891914
Startup modelType of model: OTHER
Final reconstructionNumber classes used: 7 / Applied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 3.1) / Number images used: 278030
Initial angle assignmentType: OTHER / Software - Name: RELION (ver. 3.1)
Final angle assignmentType: OTHER / Software - Name: RELION (ver. 3.1)
Final 3D classificationNumber classes: 8 / Software - Name: RELION (ver. 3.1)
FSC plot (resolution estimation)

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