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- PDB-1ljz: NMR structure of an AChR-peptide (Torpedo Californica, alpha-subu... -

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Basic information

Entry
Database: PDB / ID: 1ljz
TitleNMR structure of an AChR-peptide (Torpedo Californica, alpha-subunit residues 182-202) in complex with alpha-Bungarotoxin
Components
  • Acetylcholine receptor protein
  • alpha-Bungarotoxin
KeywordsReceptor / Toxin / bungarotoxin / acetylcholine receptor / beta-hairpin / intermolecular beta-sheet
Function / homology
Function and homology information


acetylcholine receptor inhibitor activity / acetylcholine-gated monoatomic cation-selective channel activity / ion channel regulator activity / transmembrane signaling receptor activity / toxin activity / postsynaptic membrane / extracellular region
Similarity search - Function
Snake toxin and toxin-like protein / Snake three-finger toxin / Snake toxins signature. / Snake toxin, conserved site / Nicotinic acetylcholine receptor / CD59 / CD59 / Snake toxin-like superfamily / Neurotransmitter-gated ion-channel, conserved site / Neurotransmitter-gated ion-channels signature. ...Snake toxin and toxin-like protein / Snake three-finger toxin / Snake toxins signature. / Snake toxin, conserved site / Nicotinic acetylcholine receptor / CD59 / CD59 / Snake toxin-like superfamily / Neurotransmitter-gated ion-channel, conserved site / Neurotransmitter-gated ion-channels signature. / Neurotransmitter-gated ion-channel transmembrane domain / Neurotransmitter-gated ion-channel transmembrane region / Neurotransmitter-gated ion-channel transmembrane domain superfamily / Neuronal acetylcholine receptor / Neurotransmitter-gated ion-channel / Neurotransmitter-gated ion-channel ligand-binding domain / Neurotransmitter-gated ion-channel ligand-binding domain superfamily / Neurotransmitter-gated ion-channel ligand binding domain / Ribbon / Mainly Beta
Similarity search - Domain/homology
Acetylcholine receptor subunit alpha / Alpha-bungarotoxin
Similarity search - Component
Biological speciesBungarus multicinctus (many-banded krait)
MethodSOLUTION NMR / distance geometry simulated annealing energy minimization
AuthorsSamson, A.O. / Scherf, T. / Eisenstein, M. / Chill, J.H. / Anglister, J.
CitationJournal: Neuron / Year: 2002
Title: The mechanism for acetylcholine receptor inhibition by alpha-neurotoxins and species-specific resistance to alpha-bungarotoxin revealed by NMR.
Authors: Samson, A. / Scherf, T. / Eisenstein, M. / Chill, J. / Anglister, J.
History
DepositionApr 23, 2002Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 17, 2002Provider: repository / Type: Initial release
Revision 1.1Apr 28, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Jul 24, 2013Group: Other

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: alpha-Bungarotoxin
B: Acetylcholine receptor protein


Theoretical massNumber of molelcules
Total (without water)11,1432
Polymers11,1432
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)19 / 100structures with the lowest energy
Representative

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Components

#1: Protein alpha-Bungarotoxin / Long Neurotoxin 1 / Alpha-BTX / BGTX


Mass: 8005.281 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bungarus multicinctus (many-banded krait) / Secretion: venom / Strain: Banded krait / References: UniProt: P60615
#2: Protein/peptide Acetylcholine receptor protein / / AChR


Mass: 3137.432 Da / Num. of mol.: 1 / Fragment: Acetylcholine receptor peptide (residues 182-202) / Source method: obtained synthetically / Details: synthesized peptide / References: UniProt: P02711

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D TOCSY
1212D NOESY
2322D NOESY
242DQF-COSY
2522D TOCSY
NMR detailsText: This structure was determined using standard 2D homonuclear techniques

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Sample preparation

Details
Solution-IDContentsSolvent system
1acetylcholine receptor peptide/alpha-bungarotoxin90% H2O/10% D2O
2acetylcholine receptor peptide/alpha-bungarotoxin100% D2O
Sample conditions
Conditions-IDIonic strengthpHPressure (kPa)Temperature (K)
150 mM NH4Ac 4 ambient 298 K
250 mM NH4Ac 4 ambient 298 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthRelative weight: 1
NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker DRXBrukerDRX8001
Bruker DMXBrukerDMX5002

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Processing

NMR software
NameVersionDeveloperClassification
CNS1brungerrefinement
CNS1brungerstructure solution
XWINNMR3brukerdata analysis
AURELIA2.8.11neidigdata analysis
RefinementMethod: distance geometry simulated annealing energy minimization
Software ordinal: 1
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 100 / Conformers submitted total number: 19

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