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- PDB-1iiw: GLUR0 LIGAND BINDING CORE: CLOSED-CLEFT LIGAND-FREE STRUCTURE -

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Basic information

Entry
Database: PDB / ID: 1iiw
TitleGLUR0 LIGAND BINDING CORE: CLOSED-CLEFT LIGAND-FREE STRUCTURE
ComponentsSlr1257 protein
KeywordsMEMBRANE PROTEIN / FOLD RELATED TO PBPS
Function / homology
Function and homology information


ligand-gated monoatomic ion channel activity / membrane
Similarity search - Function
Bacterial periplasmic substrate-binding proteins / Potassium channel domain / Ion channel / Bacterial extracellular solute-binding proteins, family 3 / Solute-binding protein family 3/N-terminal domain of MltF / : / Ligand-gated ion channel / Ionotropic glutamate receptor / Eukaryotic homologues of bacterial periplasmic substrate binding proteins. / Periplasmic binding protein-like II ...Bacterial periplasmic substrate-binding proteins / Potassium channel domain / Ion channel / Bacterial extracellular solute-binding proteins, family 3 / Solute-binding protein family 3/N-terminal domain of MltF / : / Ligand-gated ion channel / Ionotropic glutamate receptor / Eukaryotic homologues of bacterial periplasmic substrate binding proteins. / Periplasmic binding protein-like II / D-Maltodextrin-Binding Protein; domain 2 / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
Biological speciesSynechocystis sp. PCC 6803 substr. Kazusa (bacteria)
MethodX-RAY DIFFRACTION / FOURIER SYNTHESIS / Resolution: 1.9 Å
AuthorsMayer, M.L. / Olson, R. / Gouaux, E.
Citation
Journal: J.Mol.Biol. / Year: 2001
Title: Mechanisms for ligand binding to GluR0 ion channels: crystal structures of the glutamate and serine complexes and a closed apo state.
Authors: Mayer, M.L. / Olson, R. / Gouaux, E.
#1: Journal: Nature / Year: 1999
Title: FUNCTIONAL CHARACTERIZATION OF A POTASSIUM-SELECTIVE PROKARYOTIC GLUTAMATE RECEPTOR
Authors: CHEN, G.-Q. / CUI, C. / MAYER, M.L. / GOUAUX, E.
History
DepositionApr 24, 2001Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 19, 2001Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Apr 11, 2012Group: Database references
Revision 1.4Aug 2, 2017Group: Source and taxonomy / Category: entity_src_gen
Revision 1.5Feb 7, 2024Group: Data collection / Database references
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details
Remark 999SEQUENCE NATIVE GLURO IS A MEMBRANE PROTEIN. THE PROTEIN CRYSTALLIZED BY THE AUTHOR IS THE ...SEQUENCE NATIVE GLURO IS A MEMBRANE PROTEIN. THE PROTEIN CRYSTALLIZED BY THE AUTHOR IS THE EXTRACELLULAR LIGAND BINDING DOMAIN OF GLURO. TRANSMEMBRANE REGIONS WERE GENETICALLY REMOVED AND REPLACED WITH A THR LINKER. THE SEQUENCE, AS A RESULT, MATCHES DISCONTINUOUSLY WITH THE REFERENCE DATABASE.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Slr1257 protein


Theoretical massNumber of molelcules
Total (without water)25,5661
Polymers25,5661
Non-polymers00
Water1,946108
1
A: Slr1257 protein

A: Slr1257 protein


Theoretical massNumber of molelcules
Total (without water)51,1322
Polymers51,1322
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_755-x+2,y,-z1
Unit cell
Length a, b, c (Å)97.258, 49.483, 56.374
Angle α, β, γ (deg.)90.00, 117.32, 90.00
Int Tables number5
Space group name H-MC121

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Components

#1: Protein Slr1257 protein


Mass: 25565.977 Da / Num. of mol.: 1
Fragment: GLUR0 LIGAND BINDING CORE, RESIDUES 44-140, 256-385
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Synechocystis sp. PCC 6803 substr. Kazusa (bacteria)
Strain: PCC 6803 / Kazusa / Gene: GluR0 slr1257, slr1257 / Plasmid: pETGQ / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P73797
#2: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 108 / 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: 2.36 Å3/Da / Density % sol: 47.79 %
Crystal growTemperature: 277 K / Method: vapor diffusion, hanging drop / pH: 4.8
Details: 34% MPD, 100 mM Na Acetate, 5% glycerol, pH 4.8, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Crystal grow
*PLUS
Temperature: 4 ℃ / PH range low: 4.8 / PH range high: 4.7
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-ID
110-20 mg/mlprotein1drop
234-38 %MPD1reservoir
3100 mMsodium acetate1reservoir
45 %glycerol1reservoir
55 %glycerol1drop

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Data collection

DiffractionMean temperature: 110 K
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.5418 Å
DetectorType: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Sep 15, 2000
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 1.9→20 Å / Num. all: 18964 / Num. obs: 18470 / % possible obs: 97.5 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Redundancy: 3.01 % / Biso Wilson estimate: 26.081 Å2 / Rmerge(I) obs: 0.046 / Net I/σ(I): 18
Reflection shellResolution: 1.9→1.97 Å / Redundancy: 1.9 % / Rmerge(I) obs: 0.204 / Mean I/σ(I) obs: 4.4 / % possible all: 81.1
Reflection
*PLUS
Num. measured all: 110565
Reflection shell
*PLUS
% possible obs: 81.1 %

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Processing

Software
NameVersionClassification
DMmodel building
X-PLOR3.851refinement
DENZOdata reduction
SCALEPACKdata scaling
DMphasing
RefinementMethod to determine structure: FOURIER SYNTHESIS / Resolution: 1.9→20 Å / Cross valid method: THROUGHOUT / σ(F): 2 / σ(I): 2 / Stereochemistry target values: Engh & Huber
RfactorNum. reflectionSelection details
Rfree0.266 894 RANDOM
Rwork0.21 --
obs0.213 18307 -
all-18307 -
Refinement stepCycle: LAST / Resolution: 1.9→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1675 0 0 108 1783
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_bond_d0.007
X-RAY DIFFRACTIONx_angle_deg1.252
X-RAY DIFFRACTIONx_mcbond_it1.569
X-RAY DIFFRACTIONx_mcangle_it2.451
X-RAY DIFFRACTIONx_scbond_it2.773
X-RAY DIFFRACTIONx_scangle_it4.191
X-RAY DIFFRACTIONx_dihedral_angle_d23.9
X-RAY DIFFRACTIONx_improper_angle_d1.21
LS refinement shellResolution: 1.9→1.99 Å
RfactorNum. reflection
Rfree0.321 91
Rwork0.351 -
obs-1943
Software
*PLUS
Name: X-PLOR / Version: 3.851 / Classification: refinement
Refinement
*PLUS
Lowest resolution: 20 Å / σ(F): 2 / Rfactor Rwork: 0.21
Solvent computation
*PLUS
Displacement parameters
*PLUS
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_dihedral_angle_d
X-RAY DIFFRACTIONx_dihedral_angle_deg23.9
X-RAY DIFFRACTIONx_improper_angle_d
X-RAY DIFFRACTIONx_improper_angle_deg1.21
LS refinement shell
*PLUS
Rfactor Rfree: 0.321 / Rfactor Rwork: 0.351

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