[English] 日本語
![](img/lk-miru.gif)
- PDB-7smt: Cryo-EM structure of Torpedo acetylcholine receptor in complex wi... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 7smt | ||||||
---|---|---|---|---|---|---|---|
Title | Cryo-EM structure of Torpedo acetylcholine receptor in complex with d-tubocurarine and carbachol | ||||||
![]() | (Acetylcholine receptor subunit ...) x 4 | ||||||
![]() | TRANSPORT PROTEIN / acetylcholine receptor / nicotinic receptor / Torpedo / Cys-loop receptor / ion channel / muscle-type nicotinic receptor | ||||||
Function / homology | ![]() acetylcholine-gated monoatomic cation-selective channel activity / transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential / transmembrane signaling receptor activity / postsynaptic membrane / neuron projection Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.56 Å | ||||||
![]() | Rahman, M.M. / Basta, T. / Teng, J. / Lee, M. / Worrell, B.T. / Stowell, M.H.B. / Hibbs, R.E. | ||||||
Funding support | ![]()
| ||||||
![]() | ![]() Title: Structural mechanism of muscle nicotinic receptor desensitization and block by curare. Authors: Md Mahfuzur Rahman / Tamara Basta / Jinfeng Teng / Myeongseon Lee / Brady T Worrell / Michael H B Stowell / Ryan E Hibbs / ![]() Abstract: Binding of the neurotransmitter acetylcholine to its receptors on muscle fibers depolarizes the membrane and thereby triggers muscle contraction. We sought to understand at the level of three- ...Binding of the neurotransmitter acetylcholine to its receptors on muscle fibers depolarizes the membrane and thereby triggers muscle contraction. We sought to understand at the level of three-dimensional structure how agonists and antagonists alter nicotinic acetylcholine receptor conformation. We used the muscle-type receptor from the Torpedo ray to first define the structure of the receptor in a resting, activatable state. We then determined the receptor structure bound to the agonist carbachol, which stabilizes an asymmetric, closed channel desensitized state. We find conformational changes in a peripheral membrane helix are tied to recovery from desensitization. To probe mechanisms of antagonism, we obtained receptor structures with the active component of curare, a poison arrow toxin and precursor to modern muscle relaxants. d-Tubocurarine stabilizes the receptor in a desensitized-like state in the presence and absence of agonist. These findings define the transitions between resting and desensitized states and reveal divergent means by which antagonists block channel activity of the muscle-type nicotinic receptor. | ||||||
History |
|
-
Structure visualization
Movie |
![]() |
---|---|
Structure viewer | Molecule: ![]() ![]() |
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 381.2 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 318.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.4 MB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 1.4 MB | Display | |
Data in XML | ![]() | 62.3 KB | Display | |
Data in CIF | ![]() | 94 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 25208MC ![]() 7smmC ![]() 7smqC ![]() 7smrC ![]() 7smsC M: map data used to model this data C: citing same article ( |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
|
---|---|
1 |
|
-
Components
-Acetylcholine receptor subunit ... , 4 types, 5 molecules ADBCE
#1: Protein | Mass: 50168.164 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() ![]() References: UniProt: P02710 #2: Protein | | Mass: 57625.711 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() ![]() References: UniProt: P02718 #3: Protein | | Mass: 53731.773 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() ![]() References: UniProt: P02712 #4: Protein | | Mass: 56335.684 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() ![]() References: UniProt: P02714 |
---|
-Sugars , 4 types, 7 molecules ![](data/chem/img/NAG.gif)
#5: Polysaccharide | Source method: isolated from a genetically manipulated source #6: Polysaccharide | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose | Source method: isolated from a genetically manipulated source #7: Polysaccharide | beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta- ...beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose | Source method: isolated from a genetically manipulated source #11: Sugar | |
---|
-Non-polymers , 5 types, 11 molecules ![](data/chem/img/CCE.gif)
![](data/chem/img/CLR.gif)
![](data/chem/img/POV.gif)
![](data/chem/img/DD9.gif)
![](data/chem/img/TC9.gif)
![](data/chem/img/CLR.gif)
![](data/chem/img/POV.gif)
![](data/chem/img/DD9.gif)
![](data/chem/img/TC9.gif)
#8: Chemical | ChemComp-CCE / | ||||||
---|---|---|---|---|---|---|---|
#9: Chemical | #10: Chemical | ChemComp-POV / ( #12: Chemical | ChemComp-DD9 / | #13: Chemical | ChemComp-TC9 / | |
-Details
Has ligand of interest | Y |
---|
-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
---|---|
EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-
Sample preparation
Component | Name: Torpedo acetylcholine receptor in complex with d-tubocurarine and carbachol Type: COMPLEX / Entity ID: #1-#4 / Source: NATURAL |
---|---|
Source (natural) | Organism: ![]() ![]() |
Buffer solution | pH: 7.4 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
-
Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
---|---|
Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD |
Image recording | Electron dose: 35 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
-
Processing
Software | Name: PHENIX / Version: 1.19.2_4158: / Classification: refinement | ||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
EM software |
| ||||||||||||||||||||||||
CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
3D reconstruction | Resolution: 2.56 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 318847 / Symmetry type: POINT | ||||||||||||||||||||||||
Refinement | Highest resolution: 2.56 Å | ||||||||||||||||||||||||
Refine LS restraints |
|