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- PDB-3tls: The GLIC pentameric Ligand-Gated Ion Channel E19'P mutant in a lo... -

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Basic information

Entry
Database: PDB / ID: 3tls
TitleThe GLIC pentameric Ligand-Gated Ion Channel E19'P mutant in a locally-closed conformation (LC2 subtype)
ComponentsGlr4197 protein
KeywordsMEMBRANE PROTEIN / TRANSPORT PROTEIN / Cys-loop receptor family
Function / homology
Function and homology information


sodium channel activity / potassium channel activity / transmembrane transporter complex / extracellular ligand-gated monoatomic ion channel activity / transmembrane signaling receptor activity / identical protein binding / plasma membrane
Similarity search - Function
Neurotransmitter-gated ion-channel transmembrane domain / Acetylcholine Binding Protein; Chain: A, / Neurotransmitter-gated ion-channel ligand-binding domain / Gamma-aminobutyric acid A receptor/Glycine receptor alpha / 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 ...Neurotransmitter-gated ion-channel transmembrane domain / Acetylcholine Binding Protein; Chain: A, / Neurotransmitter-gated ion-channel ligand-binding domain / Gamma-aminobutyric acid A receptor/Glycine receptor alpha / 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 / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / Distorted Sandwich / Up-down Bundle / Mainly Beta / Mainly Alpha
Similarity search - Domain/homology
Proton-gated ion channel
Similarity search - Component
Biological speciesGloeobacter violaceus (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.2 Å
AuthorsSauguet, L. / Nury, H. / Corringer, P.J. / Delarue, M.
CitationJournal: Nat.Struct.Mol.Biol. / Year: 2012
Title: A locally closed conformation of a bacterial pentameric proton-gated ion channel.
Authors: Prevost, M.S. / Sauguet, L. / Nury, H. / Van Renterghem, C. / Huon, C. / Poitevin, F. / Baaden, M. / Delarue, M. / Corringer, P.J.
History
DepositionAug 30, 2011Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 16, 2012Provider: repository / Type: Initial release
Revision 1.1May 30, 2012Group: Database references
Revision 1.2Jun 27, 2012Group: Database references
Revision 1.3Feb 28, 2024Group: Data collection / Database references / Derived calculations
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Glr4197 protein
B: Glr4197 protein
C: Glr4197 protein
D: Glr4197 protein
E: Glr4197 protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)183,41811
Polymers182,7305
Non-polymers6886
Water84747
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area23660 Å2
ΔGint-206 kcal/mol
Surface area62720 Å2
MethodPISA
Unit cell
Length a, b, c (Å)180.272, 131.074, 158.139
Angle α, β, γ (deg.)90.000, 101.920, 90.000
Int Tables number5
Space group name H-MC121

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Components

#1: Protein
Glr4197 protein / GLIC


Mass: 36546.039 Da / Num. of mol.: 5 / Fragment: UNP residues 44-359 / Mutation: E285P
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Gloeobacter violaceus (bacteria) / Gene: glr4197 / Production host: Escherichia coli (E. coli) / References: UniProt: Q7NDN8
#2: Chemical
ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: Cl
#3: Sugar ChemComp-LMT / DODECYL-BETA-D-MALTOSIDE


Type: D-saccharide / Mass: 510.615 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C24H46O11 / Comment: detergent*YM
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 47 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 5.001977 Å3/Da / Density % sol: 75.409721 %
Crystal growTemperature: 293 K / Method: vapor diffusion / pH: 4 / Details: pH 4, VAPOR DIFFUSION, temperature 293K

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Data collection

Diffraction sourceSource: SYNCHROTRON / Site: SOLEIL / Beamline: PROXIMA 1 / Wavelength: 0.9919 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD
RadiationMonochromator: channel cut / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9919 Å / Relative weight: 1
ReflectionResolution: 3.2→44.21 Å / Num. obs: 58339 / % possible obs: 98.5 % / Redundancy: 3.1 % / Biso Wilson estimate: 76.1 Å2 / Rmerge(I) obs: 0.121 / Rsym value: 0.081 / Net I/σ(I): 7.4
Reflection shellResolution: 3.2→3.37 Å / Redundancy: 3.1 % / Rmerge(I) obs: 0.75 / Mean I/σ(I) obs: 2 / Num. unique all: 8177 / Rsym value: 0.497 / % possible all: 94.7

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Processing

Software
NameVersionClassificationNB
BUSTER-TNTBUSTER 2.11.1refinement
PDB_EXTRACT3.1data extraction
SCALAdata scaling
BUSTER2.11.1refinement
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 3.2→44.21 Å / Cor.coef. Fo:Fc: 0.8679 / Cor.coef. Fo:Fc free: 0.8289 / Occupancy max: 1 / Occupancy min: 1 / SU R Cruickshank DPI: 0.844 / Cross valid method: THROUGHOUT / σ(F): 0 / SU R Blow DPI: 0.686 / SU Rfree Blow DPI: 0.329 / SU Rfree Cruickshank DPI: 0.345
RfactorNum. reflection% reflectionSelection details
Rfree0.2302 2943 5.04 %RANDOM
Rwork0.2033 ---
obs0.2046 58339 98.1 %-
Displacement parametersBiso max: 183.3 Å2 / Biso mean: 81.0238 Å2 / Biso min: 27.91 Å2
Baniso -1Baniso -2Baniso -3
1--13.1753 Å20 Å235.2816 Å2
2---1.9064 Å20 Å2
3---15.0817 Å2
Refine analyzeLuzzati coordinate error obs: 0.634 Å
Refinement stepCycle: LAST / Resolution: 3.2→44.21 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms12615 0 17 47 12679
Refine LS restraints
Refine-IDTypeNumberRestraint functionWeightDev ideal
X-RAY DIFFRACTIONt_dihedral_angle_d4289SINUSOIDAL2
X-RAY DIFFRACTIONt_trig_c_planes255HARMONIC2
X-RAY DIFFRACTIONt_gen_planes1870HARMONIC5
X-RAY DIFFRACTIONt_it12971HARMONIC20
X-RAY DIFFRACTIONt_chiral_improper_torsion1760SEMIHARMONIC5
X-RAY DIFFRACTIONt_ideal_dist_contact14904SEMIHARMONIC4
X-RAY DIFFRACTIONt_bond_d12971HARMONIC20.01
X-RAY DIFFRACTIONt_angle_deg17735HARMONIC21.1
X-RAY DIFFRACTIONt_omega_torsion2.78
X-RAY DIFFRACTIONt_other_torsion19.87
LS refinement shellResolution: 3.2→3.28 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.2979 191 4.99 %
Rwork0.2632 3633 -
all0.2649 3824 -
obs--98.1 %

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