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- EMDB-8290: GluK2EM with LY466195 -

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Basic information

Entry
Database: EMDB / ID: EMD-8290
TitleGluK2EM with LY466195
Map dataGluK2EM with LY466195
Sample
  • Complex: GluK2EM with LY466195
    • Protein or peptide: Glutamate receptor ionotropic, kainate 2
  • Ligand: (3S,4aR,6S,8aR)-6-{[(2S)-2-carboxy-4,4-difluoropyrrolidin-1-yl]methyl}decahydroisoquinoline-3-carboxylic acid
KeywordsGluK2EM with LY466195 / SIGNALING PROTEIN
Function / homology
Function and homology information


mossy fiber rosette / detection of cold stimulus involved in thermoception / Activation of Na-permeable kainate receptors / kainate selective glutamate receptor complex / Activation of Ca-permeable Kainate Receptor / negative regulation of synaptic transmission, glutamatergic / regulation of short-term neuronal synaptic plasticity / inhibitory postsynaptic potential / glutamate receptor activity / ubiquitin conjugating enzyme binding ...mossy fiber rosette / detection of cold stimulus involved in thermoception / Activation of Na-permeable kainate receptors / kainate selective glutamate receptor complex / Activation of Ca-permeable Kainate Receptor / negative regulation of synaptic transmission, glutamatergic / regulation of short-term neuronal synaptic plasticity / inhibitory postsynaptic potential / glutamate receptor activity / ubiquitin conjugating enzyme binding / receptor clustering / modulation of excitatory postsynaptic potential / neuronal action potential / regulation of JNK cascade / kainate selective glutamate receptor activity / ionotropic glutamate receptor complex / extracellularly glutamate-gated ion channel activity / behavioral fear response / positive regulation of synaptic transmission / glutamate-gated receptor activity / ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential / excitatory postsynaptic potential / hippocampal mossy fiber to CA3 synapse / presynaptic modulation of chemical synaptic transmission / regulation of membrane potential / dendrite cytoplasm / SNARE binding / transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential / synaptic transmission, glutamatergic / PDZ domain binding / postsynaptic density membrane / regulation of long-term neuronal synaptic plasticity / modulation of chemical synaptic transmission / terminal bouton / intracellular calcium ion homeostasis / positive regulation of neuron apoptotic process / presynaptic membrane / chemical synaptic transmission / perikaryon / postsynaptic membrane / scaffold protein binding / neuron apoptotic process / negative regulation of neuron apoptotic process / postsynaptic density / axon / dendrite / neuronal cell body / glutamatergic synapse / synapse / ubiquitin protein ligase binding / membrane / identical protein binding / plasma membrane
Similarity search - Function
Ionotropic glutamate receptor, metazoa / Ligated ion channel L-glutamate- and glycine-binding site / : / Ligand-gated ion channel / Ionotropic glutamate receptor, L-glutamate and glycine-binding domain / Ligated ion channel L-glutamate- and glycine-binding site / 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 ionotropic, kainate 2
Similarity search - Component
Biological speciesRattus norvegicus (Norway rat)
Methodsingle particle reconstruction / cryo EM / Resolution: 11.6 Å
AuthorsMeyerson JR / Chittori S
CitationJournal: Nature / Year: 2016
Title: Structural basis of kainate subtype glutamate receptor desensitization.
Authors: Joel R Meyerson / Sagar Chittori / Alan Merk / Prashant Rao / Tae Hee Han / Mihaela Serpe / Mark L Mayer / Sriram Subramaniam /
Abstract: Glutamate receptors are ligand-gated tetrameric ion channels that mediate synaptic transmission in the central nervous system. They are instrumental in vertebrate cognition and their dysfunction ...Glutamate receptors are ligand-gated tetrameric ion channels that mediate synaptic transmission in the central nervous system. They are instrumental in vertebrate cognition and their dysfunction underlies diverse diseases. In both the resting and desensitized states of AMPA and kainate receptor subtypes, the ion channels are closed, whereas the ligand-binding domains, which are physically coupled to the channels, adopt markedly different conformations. Without an atomic model for the desensitized state, it is not possible to address a central problem in receptor gating: how the resting and desensitized receptor states both display closed ion channels, although they have major differences in the quaternary structure of the ligand-binding domain. Here, by determining the structure of the kainate receptor GluK2 subtype in its desensitized state by cryo-electron microscopy (cryo-EM) at 3.8 Å resolution, we show that desensitization is characterized by the establishment of a ring-like structure in the ligand-binding domain layer of the receptor. Formation of this 'desensitization ring' is mediated by staggered helix contacts between adjacent subunits, which leads to a pseudo-four-fold symmetric arrangement of the ligand-binding domains, illustrating subtle changes in symmetry that are important for the gating mechanism. Disruption of the desensitization ring is probably the key switch that enables restoration of the receptor to its resting state, thereby completing the gating cycle.
History
DepositionAug 19, 2016-
Header (metadata) releaseSep 7, 2016-
Map releaseSep 7, 2016-
UpdateMar 6, 2024-
Current statusMar 6, 2024Processing site: RCSB / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.00704
  • Imaged by UCSF Chimera
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  • Surface view colored by height
  • Surface level: 0.00704
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-5kuh
  • Surface level: 0.00704
  • Imaged by UCSF Chimera
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  • Simplified surface model + fitted atomic model
  • Atomic modelsPDB-5kuh
  • Imaged by Jmol
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_8290.png

Downloads & links

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Map

FileDownload / File: emd_8290.map.gz / Format: CCP4 / Size: 103 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationGluK2EM with LY466195
Voxel sizeX=Y=Z: 1.324 Å
Density
Contour LevelBy AUTHOR: 0.00704 / Movie #1: 0.00704
Minimum - Maximum-0.005991295 - 0.030794326
Average (Standard dev.)0.00018283566 (±0.0022159251)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions300300300
Spacing300300300
CellA=B=C: 397.2 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.3241.3241.324
M x/y/z300300300
origin x/y/z0.0000.0000.000
length x/y/z397.200397.200397.200
α/β/γ90.00090.00090.000
start NX/NY/NZ-152-37
NX/NY/NZ998271
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS300300300
D min/max/mean-0.0060.0310.000

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Supplemental data

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Sample components

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Entire : GluK2EM with LY466195

EntireName: GluK2EM with LY466195
Components
  • Complex: GluK2EM with LY466195
    • Protein or peptide: Glutamate receptor ionotropic, kainate 2
  • Ligand: (3S,4aR,6S,8aR)-6-{[(2S)-2-carboxy-4,4-difluoropyrrolidin-1-yl]methyl}decahydroisoquinoline-3-carboxylic acid

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Supramolecule #1: GluK2EM with LY466195

SupramoleculeName: GluK2EM with LY466195 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1
Source (natural)Organism: Rattus norvegicus (Norway rat)

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Macromolecule #1: Glutamate receptor ionotropic, kainate 2

MacromoleculeName: Glutamate receptor ionotropic, kainate 2 / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Rattus norvegicus (Norway rat)
Molecular weightTheoretical: 85.526094 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: TTHVLRFGGI FEYVESGPMG AEELAFRFAV NTINRNRTLL PNTTLTYDTQ KINLYDSFEA SKKACDQLSL GVAAIFGPSH SSSANAVQS ICNALGVPHI QTRWKHQVSD NKDSFYVSLY PDFSSLSRAI LDLVQFFKWK TVTVVYDDST GLIRLQELIK A PSRYNLRL ...String:
TTHVLRFGGI FEYVESGPMG AEELAFRFAV NTINRNRTLL PNTTLTYDTQ KINLYDSFEA SKKACDQLSL GVAAIFGPSH SSSANAVQS ICNALGVPHI QTRWKHQVSD NKDSFYVSLY PDFSSLSRAI LDLVQFFKWK TVTVVYDDST GLIRLQELIK A PSRYNLRL KIRQLPADTK DAKPLLKEMK RGKEFHVIFD CSHEMAAGIL KQALAMGMMT EYYHYIFTTL DLFALDVEPY RY SGVNMTG FRILNTENTQ VSSIIEKWSM ERLQAPPKPD SGLLDGFMTT DAALMYDAVH VVSVAVQQFP QMTVSSLQCN RHK PWRFGT RFMSLIKEAH WEGLTGRITF NKTNGLRTDF DLDVISLKEE GLEKIGTWDP ASGLNMTESQ KGKPANITDS LSNR SLIVT TILEEPYVLF KKSDKPLYGN DRFEGYCIDL LRELSTILGF TYEIRLVEDG KYGAQDDVNG QWNGMVRELI DHKAD LAVA PLTITYVREK VIDFSKPFMT LGISILYRKG TPIDSADDLA KQTKIEYGAV EDGSTMTFFK KSKISTYDKM WAFMSS RRQ SVLVKSSEEG IQRVLTSDYA LLMESTTIEF VTQRNCNLTQ IGGLIDSKGY GVGTPMGSPY RDKITIAILQ LQEEGKL HM MKEKWWRGNG CPEEESKEAS ALGVQNIGGI FIVLAAGLVL SVFVAVGEFL YKSKKNAQLE KRSFCSAMVE ELRMSLKC Q RRLKHKPQAP VIVKTEEVIN MHTFNDRRLP GKETMA

UniProtKB: Glutamate receptor ionotropic, kainate 2, Glutamate receptor ionotropic, kainate 2

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Macromolecule #2: (3S,4aR,6S,8aR)-6-{[(2S)-2-carboxy-4,4-difluoropyrrolidin-1-yl]me...

MacromoleculeName: (3S,4aR,6S,8aR)-6-{[(2S)-2-carboxy-4,4-difluoropyrrolidin-1-yl]methyl}decahydroisoquinoline-3-carboxylic acid
type: ligand / ID: 2 / Number of copies: 4 / Formula: LY5
Molecular weightTheoretical: 346.37 Da
Chemical component information

ChemComp-LY5:
(3S,4aR,6S,8aR)-6-{[(2S)-2-carboxy-4,4-difluoropyrrolidin-1-yl]methyl}decahydroisoquinoline-3-carboxylic 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
VitrificationCryogen name: ETHANE
DetailsGluK2

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: SUPER-RESOLUTION / Average electron dose: 45.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: EMDB MAP
Initial angle assignmentType: OTHER / Software - Name: RELION (ver. 1.3)
Final angle assignmentType: OTHER / Software - Name: RELION (ver. 1.3)
Final reconstructionResolution.type: BY AUTHOR / Resolution: 11.6 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 1.3) / Number images used: 31000

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