+Open data
-Basic information
Entry | Database: PDB / ID: 6oij | ||||||
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Title | Muscarinic acetylcholine receptor 1-G11 protein complex | ||||||
Components |
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Keywords | SIGNALING PROTEIN / G-protein coupled receptor-G-protein complex / neurotransmitter receptor | ||||||
Function / homology | Function and homology information regulation of melanocyte differentiation / guanyl nucleotide binding / saliva secretion / regulation of glial cell proliferation / positive regulation of monoatomic ion transport / Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion / Muscarinic acetylcholine receptors / Acetylcholine regulates insulin secretion / endothelin receptor signaling pathway / ion channel modulating, G protein-coupled receptor signaling pathway ...regulation of melanocyte differentiation / guanyl nucleotide binding / saliva secretion / regulation of glial cell proliferation / positive regulation of monoatomic ion transport / Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion / Muscarinic acetylcholine receptors / Acetylcholine regulates insulin secretion / endothelin receptor signaling pathway / ion channel modulating, G protein-coupled receptor signaling pathway / phospholipase C-activating G protein-coupled acetylcholine receptor signaling pathway / developmental pigmentation / G protein-coupled acetylcholine receptor activity / neuromuscular synaptic transmission / cellular response to pH / cholinergic synapse / PLC beta mediated events / phospholipase C-activating dopamine receptor signaling pathway / cranial skeletal system development / adenylate cyclase-inhibiting G protein-coupled acetylcholine receptor signaling pathway / entrainment of circadian clock / positive regulation of intracellular protein transport / phosphatidylinositol phospholipase C activity / phototransduction, visible light / G protein-coupled serotonin receptor activity / : / regulation of locomotion / postsynaptic modulation of chemical synaptic transmission / action potential / ligand-gated ion channel signaling pathway / G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger / photoreceptor outer segment / regulation of postsynaptic membrane potential / enzyme regulator activity / axon terminus / G protein activity / skeletal system development / G protein-coupled receptor binding / postsynaptic density membrane / regulation of blood pressure / G-protein beta/gamma-subunit complex binding / Olfactory Signaling Pathway / Activation of the phototransduction cascade / adenylate cyclase-modulating G protein-coupled receptor signaling pathway / G beta:gamma signalling through PLC beta / Presynaptic function of Kainate receptors / positive regulation of insulin secretion / Schaffer collateral - CA1 synapse / Thromboxane signalling through TP receptor / G protein-coupled acetylcholine receptor signaling pathway / G-protein activation / Activation of G protein gated Potassium channels / Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits / Prostacyclin signalling through prostacyclin receptor / Glucagon signaling in metabolic regulation / G beta:gamma signalling through CDC42 / cognition / ADP signalling through P2Y purinoceptor 12 / G beta:gamma signalling through BTK / Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1) / Sensory perception of sweet, bitter, and umami (glutamate) taste / photoreceptor disc membrane / Adrenaline,noradrenaline inhibits insulin secretion / Glucagon-type ligand receptors / Vasopressin regulates renal water homeostasis via Aquaporins / G alpha (z) signalling events / cellular response to catecholamine stimulus / Glucagon-like Peptide-1 (GLP1) regulates insulin secretion / ADORA2B mediated anti-inflammatory cytokines production / sensory perception of taste / ADP signalling through P2Y purinoceptor 1 / adenylate cyclase-activating dopamine receptor signaling pathway / G beta:gamma signalling through PI3Kgamma / cellular response to prostaglandin E stimulus / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / GPER1 signaling / G-protein beta-subunit binding / Inactivation, recovery and regulation of the phototransduction cascade / heterotrimeric G-protein complex / G alpha (12/13) signalling events / extracellular vesicle / signaling receptor complex adaptor activity / Thrombin signalling through proteinase activated receptors (PARs) / GTPase binding / retina development in camera-type eye / Ca2+ pathway / nervous system development / presynaptic membrane / heart development / phospholipase C-activating G protein-coupled receptor signaling pathway / G alpha (i) signalling events / fibroblast proliferation / G alpha (s) signalling events / G alpha (q) signalling events / Ras protein signal transduction / chemical synaptic transmission / Extra-nuclear estrogen signaling / cell population proliferation / G protein-coupled receptor signaling pathway / lysosomal membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) Mus musculus (house mouse) | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.3 Å | ||||||
Authors | Maeda, S. / Qianhui, Q. / Skiniotis, G. / Kobilka, B. | ||||||
Funding support | United States, 1items
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Citation | Journal: 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. | ||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | Molecule: MolmilJmol/JSmol |
-Downloads & links
-Download
PDBx/mmCIF format | 6oij.cif.gz | 213.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6oij.ent.gz | 169.6 KB | Display | PDB format |
PDBx/mmJSON format | 6oij.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 6oij_validation.pdf.gz | 910.6 KB | Display | wwPDB validaton report |
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Full document | 6oij_full_validation.pdf.gz | 922.5 KB | Display | |
Data in XML | 6oij_validation.xml.gz | 34.8 KB | Display | |
Data in CIF | 6oij_validation.cif.gz | 54.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/oi/6oij ftp://data.pdbj.org/pub/pdb/validation_reports/oi/6oij | HTTPS FTP |
-Related structure data
Related structure data | 20078MC 6oikC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
-Guanine nucleotide-binding protein ... , 3 types, 3 molecules ABG
#1: Protein | Mass: 41271.086 Da / Num. of mol.: 1 Mutation: chimeric protein between G-alpha1i(1-29) and G-alpha11(30-) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: GNAI1, GNA11, GA11 / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: A0A3B3ITX3, UniProt: P29992 |
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#4: Protein | 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 |
#5: Protein | 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 |
-Protein / Antibody , 2 types, 2 molecules RH
#2: Protein | Mass: 41241.262 Da / Num. of mol.: 1 / Mutation: N11Q, N21Q Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CHRM1 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: P11229 |
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#3: Antibody | 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) |
-Non-polymers , 2 types, 3 molecules
#6: Chemical | ChemComp-IXO / |
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#7: Chemical |
-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-Sample preparation
Component |
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Molecular weight | Value: 0.15 MDa / Experimental value: NO | ||||||||||||||||||||||||
Source (natural) |
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Source (recombinant) |
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Buffer solution | pH: 7.5 | ||||||||||||||||||||||||
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||
Specimen support | Details: unspecified | ||||||||||||||||||||||||
Vitrification | Cryogen name: ETHANE |
-Electron microscopy imaging
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
Electron lens | Mode: BRIGHT FIELD |
Image recording | Electron dose: 7 e/Å2 / Detector mode: COUNTING / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
-Processing
EM software | Name: RELION / Version: 2.1 / Category: image acquisition |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
Symmetry | Point symmetry: C1 (asymmetric) |
3D reconstruction | Resolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 277988 / Symmetry type: POINT |