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- PDB-6r82: Crystal structure of the TLDc domain of Skywalker/TBC1D24 from Dr... -

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Basic information

Entry
Database: PDB / ID: 6r82
TitleCrystal structure of the TLDc domain of Skywalker/TBC1D24 from Drosophila melanogaster
ComponentsGTPase-activating protein skywalker
KeywordsUNKNOWN FUNCTION / tldc domain
Function / homology
Function and homology information


synaptic vesicle endosomal processing / negative regulation of synaptic vesicle recycling / synaptic vesicle recycling via endosome / vesicle-mediated transport in synapse / neuromuscular synaptic transmission / negative regulation of neurotransmitter secretion / regulation of GTPase activity / GTPase activator activity / neuromuscular junction / terminal bouton ...synaptic vesicle endosomal processing / negative regulation of synaptic vesicle recycling / synaptic vesicle recycling via endosome / vesicle-mediated transport in synapse / neuromuscular synaptic transmission / negative regulation of neurotransmitter secretion / regulation of GTPase activity / GTPase activator activity / neuromuscular junction / terminal bouton / synaptic vesicle membrane / neuron projection development / chemical synaptic transmission / postsynapse / endosome membrane / lipid binding / synapse / cytoplasm
Similarity search - Function
TLDc domain profile. / TLDc domain / TLD / domain in TBC and LysM domain containing proteins / Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs. / Rab-GTPase-TBC domain / Rab-GTPase-TBC domain superfamily / Rab-GTPase-TBC domain / TBC/rab GAP domain profile.
Similarity search - Domain/homology
GTPase-activating protein skywalker
Similarity search - Component
Biological speciesDrosophila melanogaster (fruit fly)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.046 Å
AuthorsFischer, B. / Paesmans, J. / Versees, W.
Funding support Belgium, 1items
OrganizationGrant numberCountry
Research Foundation - Flanders Belgium
CitationJournal: Brain / Year: 2019
Title: TBC1D24-TLDc-related epilepsy exercise-induced dystonia: rescue by antioxidants in a disease model.
Authors: Luthy, K. / Mei, D. / Fischer, B. / De Fusco, M. / Swerts, J. / Paesmans, J. / Parrini, E. / Lubarr, N. / Meijer, I.A. / Mackenzie, K.M. / Lee, W.T. / Cittaro, D. / Aridon, P. / Schoovaerts, ...Authors: Luthy, K. / Mei, D. / Fischer, B. / De Fusco, M. / Swerts, J. / Paesmans, J. / Parrini, E. / Lubarr, N. / Meijer, I.A. / Mackenzie, K.M. / Lee, W.T. / Cittaro, D. / Aridon, P. / Schoovaerts, N. / Versees, W. / Verstreken, P. / Casari, G. / Guerrini, R.
History
DepositionMar 30, 2019Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jul 17, 2019Provider: repository / Type: Initial release
Revision 1.1Aug 7, 2019Group: Data collection / Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.2Jan 24, 2024Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: GTPase-activating protein skywalker
B: GTPase-activating protein skywalker


Theoretical massNumber of molelcules
Total (without water)43,1472
Polymers43,1472
Non-polymers00
Water2,144119
1
A: GTPase-activating protein skywalker


Theoretical massNumber of molelcules
Total (without water)21,5731
Polymers21,5731
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: GTPase-activating protein skywalker


Theoretical massNumber of molelcules
Total (without water)21,5731
Polymers21,5731
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)89.483, 89.483, 135.069
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number96
Space group name H-MP43212

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Components

#1: Protein GTPase-activating protein skywalker


Mass: 21573.471 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Drosophila melanogaster (fruit fly) / Gene: sky, CG9339 / Production host: Escherichia coli (E. coli) / References: UniProt: Q9VIH7
#2: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 119 / 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: 3.13 Å3/Da / Density % sol: 60.74 %
Crystal growTemperature: 277 K / Method: vapor diffusion, hanging drop
Details: 28% PEG 3350, 0.1 M Hepes pH 7.5 and 0.6M ammonium citrate

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SOLEIL / Beamline: PROXIMA 2 / Wavelength: 0.9789 Å
DetectorType: DECTRIS EIGER X 9M / Detector: PIXEL / Date: Nov 21, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9789 Å / Relative weight: 1
ReflectionResolution: 2.046→42.38 Å / Num. obs: 35238 / % possible obs: 99.8 % / Redundancy: 15.8 % / Rmerge(I) obs: 0.094 / Net I/σ(I): 19.2
Reflection shellResolution: 2.046→2.17 Å / Rmerge(I) obs: 0.972 / Num. unique obs: 5519 / % possible all: 99.2

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Processing

Software
NameVersionClassification
PHENIX(1.11.1_2575: ???)refinement
XDSdata reduction
SCALAdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4ACJ
Resolution: 2.046→38.369 Å / SU ML: 0.25 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 23.57
RfactorNum. reflection% reflection
Rfree0.225 1762 5 %
Rwork0.1948 --
obs0.1963 35235 99.83 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 2.046→38.369 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2833 0 0 119 2952
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0082915
X-RAY DIFFRACTIONf_angle_d0.8673949
X-RAY DIFFRACTIONf_dihedral_angle_d8.3021676
X-RAY DIFFRACTIONf_chiral_restr0.054414
X-RAY DIFFRACTIONf_plane_restr0.005500
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.0465-2.10180.37451300.3142467X-RAY DIFFRACTION98
2.1018-2.16360.33121330.26592524X-RAY DIFFRACTION100
2.1636-2.23350.26561330.24782533X-RAY DIFFRACTION100
2.2335-2.31330.24351350.22812551X-RAY DIFFRACTION100
2.3133-2.40590.25891330.21882536X-RAY DIFFRACTION100
2.4059-2.51530.26731350.20662551X-RAY DIFFRACTION100
2.5153-2.64790.3171340.22742554X-RAY DIFFRACTION100
2.6479-2.81380.27651350.22312565X-RAY DIFFRACTION100
2.8138-3.0310.26521360.23422576X-RAY DIFFRACTION100
3.031-3.33580.26831360.22322586X-RAY DIFFRACTION100
3.3358-3.81810.23011360.1862593X-RAY DIFFRACTION100
3.8181-4.8090.15191400.15432649X-RAY DIFFRACTION100
4.809-38.37610.18611460.16522788X-RAY DIFFRACTION100

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