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- PDB-6oik: Muscarinic acetylcholine receptor 2-Go complex -

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Basic information

Entry
Database: PDB / ID: 6oik
TitleMuscarinic acetylcholine receptor 2-Go complex
Components
  • (Guanine nucleotide-binding protein ...) x 3
  • Antibody fragment
  • Muscarinic acetylcholine receptor M2,Muscarinic acetylcholine receptor M2
KeywordsSIGNALING PROTEIN / G-protein coupled receptor-G-protein complex / neurotransmitter receptor
Function / homology
Function and homology information


phospholipase C-activating G protein-coupled acetylcholine receptor signaling pathway / G protein-coupled acetylcholine receptor activity / adenylate cyclase-inhibiting G protein-coupled acetylcholine receptor signaling pathway / symmetric synapse / G protein-coupled serotonin receptor activity / corticotropin-releasing hormone receptor 1 binding / cholinergic synapse / neurotransmitter receptor activity / regulation of smooth muscle contraction / mu-type opioid receptor binding ...phospholipase C-activating G protein-coupled acetylcholine receptor signaling pathway / G protein-coupled acetylcholine receptor activity / adenylate cyclase-inhibiting G protein-coupled acetylcholine receptor signaling pathway / symmetric synapse / G protein-coupled serotonin receptor activity / corticotropin-releasing hormone receptor 1 binding / cholinergic synapse / neurotransmitter receptor activity / regulation of smooth muscle contraction / mu-type opioid receptor binding / G protein-coupled serotonin receptor binding / arrestin family protein binding / cardiac muscle cell apoptotic process / sensory perception of taste / dopamine receptor signaling pathway / G-protein beta/gamma-subunit complex / cellular response to catecholamine stimulus / G protein-coupled acetylcholine receptor signaling pathway / alkylglycerophosphoethanolamine phosphodiesterase activity / G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger / rhodopsin mediated signaling pathway / adenylate cyclase-activating dopamine receptor signaling pathway / photoreceptor outer segment membrane / G-protein beta-subunit binding / photoreceptor disc membrane / spectrin binding / G-protein beta/gamma-subunit complex binding / heterotrimeric G-protein complex / axon terminus / asymmetric synapse / adenylate cyclase-modulating G protein-coupled receptor signaling pathway / G protein-coupled receptor activity / extracellular vesicle / Wnt signaling pathway, calcium modulating pathway / cellular response to prostaglandin E stimulus / regulation of heart contraction / retina development in camera-type eye / phospholipase C-activating G protein-coupled receptor signaling pathway / integral component of postsynaptic membrane / clathrin-coated vesicle membrane / GTPase binding / G protein-coupled receptor binding / photoreceptor inner segment / locomotory behavior / regulation of synaptic vesicle exocytosis / integral component of presynaptic membrane / response to virus / muscle contraction / nervous system development / cell body / cell population proliferation / lysosomal membrane / cellular response to hypoxia / chemical synaptic transmission / positive regulation of cytosolic calcium ion concentration / platelet activation / membrane organization / Ras protein signal transduction / protein folding / GTPase activity / synapse / G protein-coupled receptor signaling pathway / glutamatergic synapse / cell junction / GTP binding / neuronal cell body / dendrite / protein-containing complex binding / signal transduction / integral component of plasma membrane / go:0005623: / extracellular exosome / membrane / integral component of membrane / plasma membrane / metal ion binding / cytosol
G-protein gamma-like domain / G-protein beta WD-40 repeat / G-protein alpha subunit, group I / G-protein, beta subunit / WD40 repeat / G-protein, gamma subunit / G protein alpha subunit, helical insertion / WD40/YVTN repeat-like-containing domain superfamily / Guanine nucleotide-binding protein, beta subunit / GPCR, rhodopsin-like, 7TM ...G-protein gamma-like domain / G-protein beta WD-40 repeat / G-protein alpha subunit, group I / G-protein, beta subunit / WD40 repeat / G-protein, gamma subunit / G protein alpha subunit, helical insertion / WD40/YVTN repeat-like-containing domain superfamily / Guanine nucleotide-binding protein, beta subunit / GPCR, rhodopsin-like, 7TM / Guanine nucleotide binding protein (G-protein), alpha subunit / Muscarinic acetylcholine receptor family / WD40-repeat-containing domain / WD40 repeat, conserved site / G protein-coupled receptor, rhodopsin-like / P-loop containing nucleoside triphosphate hydrolase / WD40-repeat-containing domain superfamily / 7 transmembrane receptor (rhodopsin family) / GGL domain / G-protein alpha subunit / WD domain, G-beta repeat / G-protein gamma-like domain superfamily / Muscarinic acetylcholine receptor M2 / Transducin (heterotrimeric G protein), gamma chain / G Protein Gi Gamma 2 / Rhodopsin 7-helix transmembrane proteins / Rhopdopsin 7-helix transmembrane proteins / YVTN repeat-like/Quinoprotein amine dehydrogenase / Methylamine Dehydrogenase; Chain H / 7 Propeller / Few Secondary Structures / Irregular / Immunoglobulins / Immunoglobulin-like / Up-down Bundle / Sandwich / Mainly Beta / Mainly Alpha
Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 / Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 / Guanine nucleotide-binding protein G(o) subunit alpha / Muscarinic acetylcholine receptor M2
Biological speciesHomo sapiens (human)
Mus musculus (house mouse)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.6 Å
AuthorsMaeda, S. / Qianhui, Q. / Skiniotis, G. / Kobilka, B.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R01GM083118 United States
CitationJournal: Science / Year: 2019
Title: Structures of the M1 and M2 muscarinic acetylcholine receptor/G-protein complexes.
Authors: Shoji Maeda / Qianhui Qu / Michael J Robertson / Georgios Skiniotis / Brian K Kobilka /
Abstract: Muscarinic acetylcholine receptors are G protein-coupled receptors that respond to acetylcholine and play important signaling roles in the nervous system. There are five muscarinic receptor subtypes ...Muscarinic acetylcholine receptors are G protein-coupled receptors that respond to acetylcholine and play important signaling roles in the nervous system. There are five muscarinic receptor subtypes (M1R to M5R), which, despite sharing a high degree of sequence identity in the transmembrane region, couple to different heterotrimeric GTP-binding proteins (G proteins) to transmit signals. M1R, M3R, and M5R couple to the G family, whereas M2R and M4R couple to the G family. Here, we present and compare the cryo-electron microscopy structures of M1R in complex with G and M2R in complex with G The M1R-G complex exhibits distinct features, including an extended transmembrane helix 5 and carboxyl-terminal receptor tail that interacts with G protein. Detailed analysis of these structures provides a framework for understanding the molecular determinants of G-protein coupling selectivity.
Validation Report
SummaryFull reportAbout validation report
History
DepositionApr 9, 2019Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 8, 2019Provider: repository / Type: Initial release
Revision 1.1May 22, 2019Group: Data collection / Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.name
Revision 1.2May 29, 2019Group: Data collection / Database references / Category: citation_author / Item: _citation_author.identifier_ORCID
Revision 1.3Jan 8, 2020Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization

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Structure visualization

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Assembly

Deposited unit
R: Muscarinic acetylcholine receptor M2,Muscarinic acetylcholine receptor M2
A: Guanine nucleotide-binding protein G(o) subunit alpha
B: Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
G: Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2
H: Antibody fragment
hetero molecules


Theoretical massNumber of molelcules
Total (without water)153,3997
Polymers152,7645
Non-polymers6352
Water0
1


TypeNameSymmetry operationNumber
identity operation1_5551
Buried area9700 Å2
ΔGint-67 kcal/mol
Surface area47980 Å2

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Components

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Guanine nucleotide-binding protein ... , 3 types, 3 molecules ABG

#2: Protein Guanine nucleotide-binding protein G(o) subunit alpha


Mass: 40104.551 Da / Num. of mol.: 1 / Mutation: E9D, R10K, L13V, A18M
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: GNAO1 / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: P09471
#3: Protein Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 / Transducin beta chain 1


Mass: 37728.152 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: GNB1 / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: P62873
#4: Protein Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 / G gamma-I


Mass: 7861.143 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: GNG2 / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: P59768

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Protein / Antibody , 2 types, 2 molecules RH

#1: Protein Muscarinic acetylcholine receptor M2,Muscarinic acetylcholine receptor M2


Mass: 39729.910 Da / Num. of mol.: 1 / Mutation: N8A, N11D, N14D,N11D, N14D
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CHRM2 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: P08172
#5: Antibody Antibody fragment /


Mass: 27340.482 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Production host: Trichoplusia ni (cabbage looper)

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Non-polymers , 2 types, 2 molecules

#6: Chemical ChemComp-IXO / 4-(4,5-dihydro-1,2-oxazol-3-yloxy)-N,N,N-trimethylbut-2-yn-1-aminium / Iperoxo


Mass: 197.254 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H17N2O2
#7: Chemical ChemComp-2CU / 3-amino-5-chloro-N-cyclopropyl-4-methyl-6-[2-(4-methylpiperazin-1-yl)-2-oxoethoxy]thieno[2,3-b]pyridine-2-carboxamide / LY2119620 positive allosteric modulator of M2/M4 receptor


Mass: 437.944 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C19H24ClN5O3S

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

Component
IDNameTypeEntity IDParent-IDSource
1muscarinic acetylcholine receptor 2 in complex with heterotrimeric GoA proteinCOMPLEX1, 2, 3, 4, 50RECOMBINANT
2Muscarinic acetylcholine receptor M2COMPLEX11RECOMBINANT
3Guanine nucleotide-binding protein G(o) subunit alpha, Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1, Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2, Antibody fragmentCOMPLEX2, 3, 4, 51RECOMBINANT
Molecular weightValue: 0.15 MDa / Experimental value: NO
Source (natural)
IDEntity assembly-IDOrganismNcbi tax-ID
12Homo sapiens (human)9606
23Homo sapiens (human)9606
Source (recombinant)
IDEntity assembly-IDOrganismNcbi tax-ID
12Spodoptera frugiperda (fall armyworm)7108
23Trichoplusia ni (cabbage looper)7111
Buffer solutionpH: 7.5
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportDetails: unspecified
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELDBright-field microscopy
Image recordingElectron dose: 7 e/Å2 / Detector mode: COUNTING / Film or detector model: GATAN K2 SUMMIT (4k x 4k)

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Processing

EM softwareName: RELION / Version: 2.1 / Category: image acquisition
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 3.6 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 261730 / Symmetry type: POINT

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