[English] 日本語
![](img/lk-miru.gif)
- PDB-6uwz: Cryo-EM structure of Torpedo acetylcholine receptor in complex wi... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 6uwz | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | Cryo-EM structure of Torpedo acetylcholine receptor in complex with alpha-bungarotoxin | |||||||||
![]() |
| |||||||||
![]() | TRANSPORT PROTEIN / Nicotinic acetylcholine receptor / nicotinic receptor / Torpedo / Cys-loop receptor / ion channel / neurotoxin | |||||||||
Function / homology | ![]() acetylcholine receptor inhibitor activity / ion channel regulator activity / acetylcholine-gated monoatomic cation-selective channel activity / transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential / transmembrane signaling receptor activity / toxin activity / postsynaptic membrane / neuron projection / extracellular region Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() | |||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.69 Å | |||||||||
![]() | Rahman, M.M. / Teng, J. / Worrell, B.T. / Noveillo, C.M. / Lee, M. / Karlin, A. / Stowell, M. / Hibbs, R.E. | |||||||||
Funding support | ![]()
| |||||||||
![]() | ![]() Title: Structure of the Native Muscle-type Nicotinic Receptor and Inhibition by Snake Venom Toxins. Authors: Md Mahfuzur Rahman / Jinfeng Teng / Brady T Worrell / Colleen M Noviello / Myeongseon Lee / Arthur Karlin / Michael H B Stowell / Ryan E Hibbs / ![]() Abstract: The nicotinic acetylcholine receptor, a pentameric ligand-gated ion channel, converts the free energy of binding of the neurotransmitter acetylcholine into opening of its central pore. Here we ...The nicotinic acetylcholine receptor, a pentameric ligand-gated ion channel, converts the free energy of binding of the neurotransmitter acetylcholine into opening of its central pore. Here we present the first high-resolution structure of the receptor type found in muscle-endplate membrane and in the muscle-derived electric tissues of fish. The native receptor was purified from Torpedo electric tissue and functionally reconstituted in lipids optimal for cryo-electron microscopy. The receptor was stabilized in a closed state by the binding of α-bungarotoxin. The structure reveals the binding of a toxin molecule at each of two subunit interfaces in a manner that would block the binding of acetylcholine. It also reveals a closed gate in the ion-conducting pore, formed by hydrophobic amino acid side chains, located ∼60 Å from the toxin binding sites. The structure provides a framework for understanding gating in ligand-gated channels and how mutations in the acetylcholine receptor cause congenital myasthenic syndromes. | |||||||||
History |
|
-
Structure visualization
Movie |
![]() |
---|---|
Structure viewer | Molecule: ![]() ![]() |
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 417.5 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 336.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
---|
-Related structure data
Related structure data | ![]() 20928MC 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: 56574.094 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() ![]() References: UniProt: P02714 |
---|
-Protein , 1 types, 2 molecules FG
#5: Protein | Mass: 8005.281 Da / Num. of mol.: 2 / Source method: obtained synthetically / Source: (synth.) ![]() |
---|
-Sugars , 4 types, 8 molecules ![](data/chem/img/NAG.gif)
#6: Polysaccharide | Source method: isolated from a genetically manipulated source #7: Polysaccharide | Source method: isolated from a genetically manipulated source #8: Polysaccharide | alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1- ...alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose-(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 #10: Sugar | |
---|
-Non-polymers , 3 types, 144 molecules ![](data/chem/img/POV.gif)
![](data/chem/img/OCT.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/OCT.gif)
![](data/chem/img/HOH.gif)
#9: Chemical | ChemComp-POV / ( #11: Chemical | ChemComp-OCT / | #12: Water | ChemComp-HOH / | |
---|
-Details
Has ligand of interest | N |
---|
-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 alpha-bungarotoxin Type: COMPLEX / Entity ID: #1-#5 / Source: NATURAL |
---|---|
Molecular weight | Units: KILODALTONS/NANOMETER / Experimental value: NO |
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
EM software |
| ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||
Symmetry | Point symmetry: C1 (asymmetric) | ||||||||||||
3D reconstruction | Resolution: 2.69 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 127482 / Algorithm: BACK PROJECTION / Symmetry type: POINT |