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- PDB-5gwm: Solution structure of heterodimeric coiled-coil domain of Drosoph... -

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Basic information

Entry
Database: PDB / ID: 5gwm
TitleSolution structure of heterodimeric coiled-coil domain of Drosophila GABAB receptor 1 and 3
Components
  • Metabotropic GABA-B receptor subtype 1
  • Metabotropic GABA-B receptor subtype 3, isoform A
KeywordsSIGNALING PROTEIN / GABAB receptor / Drosophila / coiled-coil
Function / homology
Function and homology information


G protein-coupled GABA receptor activity / G protein-coupled receptor heterodimeric complex / sleep / gamma-aminobutyric acid signaling pathway / transmembrane signaling receptor activity / membrane => GO:0016020 / G protein-coupled receptor signaling pathway / membrane
Similarity search - Function
GPCR family 3, gamma-aminobutyric acid receptor, type B1 / GPCR family 3, GABA-B receptor / GPCR, family 3 / GPCR family 3, C-terminal / 7 transmembrane sweet-taste receptor of 3 GCPR / G-protein coupled receptors family 3 profile. / Receptor, ligand binding region / Receptor family ligand binding region / Periplasmic binding protein-like I
Similarity search - Domain/homology
Metabotropic GABA-B receptor subtype 1 / Metabotropic GABA-B receptor subtype 3, isoform A
Similarity search - Component
Biological speciesDrosophila melanogaster (fruit fly)
MethodSOLUTION NMR / simulated annealing
AuthorsLiu, X. / Zhang, S. / Zhang, C.X. / Liu, J.
CitationJournal: To Be Published
Title: Solution structure of heterodimeric coiled-coil domain of Drosophila GABAB receptor 1 and 3
Authors: Liu, X. / Zhang, S. / Zhang, C.X. / Liu, J.
History
DepositionSep 12, 2016Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Sep 13, 2017Provider: repository / Type: Initial release
Revision 1.1Jun 14, 2023Group: Database references / Other / Category: database_2 / pdbx_database_status
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_nmr_data

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Metabotropic GABA-B receptor subtype 1
B: Metabotropic GABA-B receptor subtype 3, isoform A


Theoretical massNumber of molelcules
Total (without water)12,2822
Polymers12,2822
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
Buried area1810 Å2
ΔGint-15 kcal/mol
Surface area8470 Å2
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 200structures with the lowest energy
RepresentativeModel #1medoid

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Components

#1: Protein Metabotropic GABA-B receptor subtype 1


Mass: 6327.121 Da / Num. of mol.: 1 / Fragment: coiled-coil domain, UNP residues 751-802
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Drosophila melanogaster (fruit fly) / Gene: GABA-B-R1, CG15274 / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: Q9BML7
#2: Protein/peptide Metabotropic GABA-B receptor subtype 3, isoform A / GABAB receptor 3 / Metabotropic GABA-B receptor subtype 3 / isoform D / isoform E / isoform G


Mass: 5954.819 Da / Num. of mol.: 1 / Fragment: coiled-coil domain, UNP residues 914-954
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Drosophila melanogaster (fruit fly) / Gene: GABA-B-R3, CG3022, Dmel_CG3022 / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: Q9VPS7

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDSample stateSpectrometer-IDType
111isotropic12D 1H-15N HSQC
121isotropic13D 1H-15N NOESY
132isotropic12D 1H-15N HSQC
142isotropic12D 1H-13C HSQC
152isotropic13D HNCO
1132isotropic13D HN(CA)CB
1142isotropic13D CBCA(CO)NH
1122isotropic13D HBHA(CO)NH
1112isotropic13D (H)CCH-TOCSY
1102isotropic13D 1H-13C NOESY
172isotropic13D C(CO)NH

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Sample preparation

Details
TypeSolution-IDContentsLabelSolvent system
solution120 mM PBS, 100 mM sodium chloride, 0.02 mg/mL sodium azide, 0.7 mM [U-99% 15N] Molecule1, 0.7 mM [U-99% 15N] Molecule2, 90% H2O/10% D2ON_sample90% H2O/10% D2O
solution220 mM PBS, 100 mM sodium chloride, 0.02 mg/mL sodium azide, 0.7 mM [U-99% 13C; U-99% 15N] Molecule1, 0.7 mM [U-99% 13C; U-99% 15N] Molecule2, 90% H2O/10% D2OCN_sample90% H2O/10% D2O
Sample
Conc. (mg/ml)ComponentIsotopic labelingSolution-ID
20 mMPBSnatural abundance1
100 mMsodium chloridenatural abundance1
0.02 mg/mLsodium azidenatural abundance1
0.7 mMMolecule1[U-99% 15N]1
0.7 mMMolecule2[U-99% 15N]1
20 mMPBSnatural abundance2
100 mMsodium chloridenatural abundance2
0.02 mg/mLsodium azidenatural abundance2
0.7 mMMolecule1[U-99% 13C; U-99% 15N]2
0.7 mMMolecule2[U-99% 13C; U-99% 15N]2
Sample conditionsIonic strength: 120 mM / Label: condition1 / pH: 7.0 / Pressure: 1 atm / Temperature: 293 K

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NMR measurement

NMR spectrometerType: Agilent DD2 / Manufacturer: Agilent / Model: DD2 / Field strength: 600 MHz

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Processing

NMR software
NameVersionDeveloperClassification
CNS1.2.1Brunger, Adams, Clore, Gros, Nilges and Readrefinement
ARIA2.2Linge, O'Donoghue and Nilgesstructure calculation
CcpNMR2.3CCPNchemical shift assignment
NMRPipe3Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Baxprocessing
RefinementMethod: simulated annealing / Software ordinal: 1
NMR representativeSelection criteria: medoid
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 200 / Conformers submitted total number: 20

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