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- PDB-2zej: Structure of the ROC domain from the Parkinson's disease-associat... -

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Basic information

Entry
Database: PDB / ID: 2zej
TitleStructure of the ROC domain from the Parkinson's disease-associated leucine-rich repeat kinase 2 reveals a dimeric GTPase
ComponentsLeucine-rich repeat kinase 2
KeywordsTRANSFERASE / Parkinson's Disease / LRRK2 / ROC / GTPase / ROCO / Kinase / ATP-binding / Disease mutation / GTP-binding / GTPase activation / Leucine-rich repeat / Membrane / Nucleotide-binding / Parkinson disease / Serine/threonine-protein kinase
Function / homology
Function and homology information


regulation of multicellular organismal process / intracellular organelle lumen / regulation of neuron maturation / caveola neck / : / beta-catenin destruction complex binding / regulation of branching morphogenesis of a nerve / Wnt signalosome assembly / negative regulation of motile cilium assembly / regulation of kidney size ...regulation of multicellular organismal process / intracellular organelle lumen / regulation of neuron maturation / caveola neck / : / beta-catenin destruction complex binding / regulation of branching morphogenesis of a nerve / Wnt signalosome assembly / negative regulation of motile cilium assembly / regulation of kidney size / regulation of cell projection organization / regulation of dopamine receptor signaling pathway / tangential migration from the subventricular zone to the olfactory bulb / regulation of ER to Golgi vesicle-mediated transport / GTP-dependent protein kinase activity / regulation of SNARE complex assembly / regulation of neuroblast proliferation / animal organ development / protein localization to endoplasmic reticulum exit site / negative regulation of late endosome to lysosome transport / regulation of mitochondrial depolarization / : / peroxidase inhibitor activity / positive regulation of dopamine receptor signaling pathway / amphisome / regulation of synaptic vesicle transport / : / regulation of CAMKK-AMPK signaling cascade / negative regulation of autophagosome assembly / co-receptor binding / positive regulation of microglial cell activation / regulation of intracellular signal transduction / olfactory bulb development / regulation of vesicle-mediated transport / regulation of retrograde transport, endosome to Golgi / negative regulation of GTPase activity / cellular response to curcumin / striatum development / regulation of locomotion / positive regulation of synaptic vesicle endocytosis / JUN kinase kinase kinase activity / cytoplasmic side of mitochondrial outer membrane / negative regulation of excitatory postsynaptic potential / regulation of cAMP/PKA signal transduction / multivesicular body, internal vesicle / endoplasmic reticulum organization / neuron projection arborization / mitochondrion localization / regulation of dendritic spine morphogenesis / protein localization to mitochondrion / positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway / cellular response to dopamine / negative regulation of protein processing / positive regulation of protein autoubiquitination / Wnt signalosome / exploration behavior / GTP metabolic process / regulation of reactive oxygen species metabolic process / regulation of canonical Wnt signaling pathway / lysosome organization / syntaxin-1 binding / positive regulation of programmed cell death / negative regulation of macroautophagy / PTK6 promotes HIF1A stabilization / Golgi-associated vesicle / clathrin binding / Golgi organization / regulation of synaptic vesicle exocytosis / regulation of mitochondrial fission / intracellular distribution of mitochondria / Lewy body / protein kinase A binding / canonical Wnt signaling pathway / microvillus / neuromuscular junction development / positive regulation of protein metabolic process / locomotory exploration behavior / autolysosome / regulation of proteolysis / endoplasmic reticulum exit site / MAP kinase kinase kinase activity / JNK cascade / regulation of synaptic vesicle endocytosis / negative regulation of signal transduction / anatomical structure morphogenesis / negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway / Rho protein signal transduction / regulation of synaptic transmission, glutamatergic / determination of adult lifespan / presynaptic cytosol / cellular response to manganese ion / vesicle-mediated transport / neuron projection morphogenesis / phagocytic vesicle / positive regulation of autophagy / dendrite cytoplasm / excitatory postsynaptic potential / positive regulation of protein ubiquitination / cellular response to starvation / regulation of autophagy
Similarity search - Function
ROC domain from the Parkinson's disease-associated leucine-rich repeat kinase 2 / : / : / : / LRRK2 ARM repeat / LRRK2 ANK repeat / LRRK2 beta propeller / : / : / C-terminal of Roc, COR-B domain ...ROC domain from the Parkinson's disease-associated leucine-rich repeat kinase 2 / : / : / : / LRRK2 ARM repeat / LRRK2 ANK repeat / LRRK2 beta propeller / : / : / C-terminal of Roc, COR-B domain / C-terminal of Roc (COR) domain / C-terminal of Roc, COR-A domain / Ras of Complex, Roc, domain of DAPkinase / Roc domain profile. / Roc domain / Small GTPase Rab domain profile. / Leucine-rich repeats, bacterial type / Leucine rich repeat / Leucine-rich repeat, typical subtype / Leucine-rich repeats, typical (most populated) subfamily / Leucine-rich repeat profile. / Leucine-rich repeat / Leucine-rich repeat domain superfamily / Rab subfamily of small GTPases / Ankyrin repeat-containing domain superfamily / Armadillo-like helical / Small GTP-binding protein domain / Armadillo-type fold / P-loop containing nucleotide triphosphate hydrolases / Alpha-Beta Plaits / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. / Protein kinase domain / Serine/Threonine protein kinases, catalytic domain / WD40-repeat-containing domain superfamily / WD40/YVTN repeat-like-containing domain superfamily / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily / Rossmann fold / P-loop containing nucleoside triphosphate hydrolase / 2-Layer Sandwich / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
GUANOSINE-5'-DIPHOSPHATE / Leucine-rich repeat serine/threonine-protein kinase 2 / Leucine-rich repeat serine/threonine-protein kinase 2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2 Å
AuthorsDeng, J.
CitationJournal: Proc.Natl.Acad.Sci.Usa / Year: 2008
Title: Structure of the ROC domain from the Parkinson's disease-associated leucine-rich repeat kinase 2 reveals a dimeric GTPase
Authors: Deng, J. / Lewis, P.A. / Greggio, E. / Sluch, E. / Beilina, A. / Cookson, M.R.
History
DepositionDec 13, 2007Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Jan 22, 2008Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Version format compliance
Revision 1.2Oct 11, 2017Group: Advisory / Refinement description / Category: pdbx_unobs_or_zero_occ_atoms / software
Revision 1.3Nov 6, 2024Group: Advisory / Data collection ...Advisory / Data collection / Database references / Derived calculations / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature / pdbx_struct_conn_angle / pdbx_unobs_or_zero_occ_atoms / struct_conn / struct_conn_type / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_conn_type.id / _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: Leucine-rich repeat kinase 2
B: Leucine-rich repeat kinase 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)43,7786
Polymers42,8432
Non-polymers9354
Water2,018112
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7850 Å2
ΔGint-81.5 kcal/mol
Surface area14510 Å2
MethodPISA
Unit cell
Length a, b, c (Å)44.438, 44.404, 53.681
Angle α, β, γ (deg.)81.51, 69.00, 78.71
Int Tables number1
Space group name H-MP1

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Components

#1: Protein Leucine-rich repeat kinase 2 / Dardarin


Mass: 21421.732 Da / Num. of mol.: 2 / Fragment: ROC-GTPase domain, UNP residues 1333-1516
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: LRRK2 / Plasmid: pSKB3 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21goldDE3
References: UniProt: Q17RV3, UniProt: Q5S007*PLUS, non-specific serine/threonine protein kinase
#2: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg
#3: Chemical ChemComp-GDP / GUANOSINE-5'-DIPHOSPHATE


Type: RNA linking / Mass: 443.201 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H15N5O11P2 / Comment: GDP, energy-carrying molecule*YM
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 112 / Source method: isolated from a natural source / Formula: H2O
Has protein modificationY

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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: 2.26 Å3/Da / Density % sol: 45.46 %
Crystal growTemperature: 298 K / Method: vapor diffusion, sitting drop / pH: 8
Details: 30% PEG 4000, 100mM MgCl2, 0.1M Tris, 5mM GTP, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 0.97948 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Jun 21, 2007
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97948 Å / Relative weight: 1
ReflectionResolution: 2→50 Å / Num. obs: 23675 / % possible obs: 93.1 % / Redundancy: 4 % / Biso Wilson estimate: 29.1 Å2 / Rmerge(I) obs: 0.126 / Net I/σ(I): 16.9
Reflection shellResolution: 2→2.03 Å / Redundancy: 1.9 % / Rmerge(I) obs: 0.398 / Mean I/σ(I) obs: 1.8 / Num. unique all: 793 / % possible all: 62.3

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Processing

Software
NameVersionClassification
REFMAC5.3.0037refinement
HKL-3000data reduction
HKL-3000data scaling
HKL-3000phasing
RefinementMethod to determine structure: SAD / Resolution: 2→38.8 Å / Cor.coef. Fo:Fc: 0.951 / Cor.coef. Fo:Fc free: 0.924 / SU B: 8.66 / SU ML: 0.14 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.198 / ESU R Free: 0.182 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.25306 1192 5.1 %RANDOM
Rwork0.19874 ---
obs0.20156 22346 93.09 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 34.29 Å2
Baniso -1Baniso -2Baniso -3
1-0.31 Å2-0.16 Å2-0.43 Å2
2---0.59 Å2-0.38 Å2
3---0.76 Å2
Refinement stepCycle: LAST / Resolution: 2→38.8 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2538 0 58 112 2708
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0170.0222601
X-RAY DIFFRACTIONr_angle_refined_deg2.1451.983530
X-RAY DIFFRACTIONr_dihedral_angle_1_deg15.9085317
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.98724.571105
X-RAY DIFFRACTIONr_dihedral_angle_3_deg20.04515455
X-RAY DIFFRACTIONr_dihedral_angle_4_deg20.3461511
X-RAY DIFFRACTIONr_chiral_restr0.270.2408
X-RAY DIFFRACTIONr_gen_planes_refined0.0070.021876
X-RAY DIFFRACTIONr_nbd_refined0.2120.21097
X-RAY DIFFRACTIONr_nbtor_refined0.3050.21725
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1390.2165
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2020.233
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.2220.28
X-RAY DIFFRACTIONr_mcbond_it1.2061.51634
X-RAY DIFFRACTIONr_mcangle_it1.73622556
X-RAY DIFFRACTIONr_scbond_it3.49731127
X-RAY DIFFRACTIONr_scangle_it4.6274.5972
LS refinement shellResolution: 2→2.052 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.32 46 -
Rwork0.222 1191 -
obs--67.34 %
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
12.23970.9937-0.69751.6663-0.24840.8813-0.0109-0.2056-0.21760.0711-0.0122-0.05120.1104-0.02940.0231-0.14220.0392-0.0209-0.0961-0.06770.056529.40337.21444.793
22.34020.8869-0.78251.9717-0.56340.83580.0136-0.00480.0275-0.1842-0.0553-0.1414-0.06090.07710.0416-0.14520.0347-0.0028-0.1007-0.08650.036744.67549.96433.221
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
1X-RAY DIFFRACTION1AA1335 - 15073 - 175
2X-RAY DIFFRACTION2BB1336 - 15104 - 178

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