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- PDB-1obz: Crystal structure of the complex of the PDZ tandem of syntenin wi... -

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Basic information

Entry
Database: PDB / ID: 1obz
TitleCrystal structure of the complex of the PDZ tandem of syntenin with an interleukin 5 receptor alpha peptide.
Components
  • INTERLEUKIN 5 RECEPTOR ALPHA
  • SYNTENIN 1
KeywordsCELL ADHESION / ADHESION-COMPLEX / PDZ DOMAIN / SIGNAL TRANSDUCTION / NUCLEAR PROTEIN
Function / homology
Function and homology information


interleukin-5 receptor activity / regulation of interleukin-5 production / interleukin-5 receptor complex / interleukin-5 receptor binding / positive regulation of extracellular exosome assembly / syndecan binding / Neurofascin interactions / presynapse assembly / neurexin family protein binding / cytoskeletal anchor activity ...interleukin-5 receptor activity / regulation of interleukin-5 production / interleukin-5 receptor complex / interleukin-5 receptor binding / positive regulation of extracellular exosome assembly / syndecan binding / Neurofascin interactions / presynapse assembly / neurexin family protein binding / cytoskeletal anchor activity / substrate-dependent cell migration, cell extension / interleukin-5-mediated signaling pathway / positive regulation of exosomal secretion / positive regulation of leukocyte proliferation / negative regulation of receptor internalization / frizzled binding / inflammatory response to antigenic stimulus / protein targeting to membrane / Ephrin signaling / cytokine receptor activity / RIPK1-mediated regulated necrosis / cytokine binding / positive regulation of transforming growth factor beta receptor signaling pathway / growth factor binding / Interleukin-3, Interleukin-5 and GM-CSF signaling / Interleukin receptor SHC signaling / positive regulation of epithelial to mesenchymal transition / positive regulation of phosphorylation / cell adhesion molecule binding / regulation of mitotic cell cycle / ionotropic glutamate receptor binding / phosphatidylinositol-4,5-bisphosphate binding / protein sequestering activity / ephrin receptor binding / positive regulation of JNK cascade / adherens junction / Regulation of necroptotic cell death / cytokine-mediated signaling pathway / azurophil granule lumen / extracellular vesicle / melanosome / presynapse / actin cytoskeleton organization / RAF/MAP kinase cascade / positive regulation of cell growth / chemical synaptic transmission / nuclear membrane / Ras protein signal transduction / blood microparticle / cytoskeleton / receptor complex / intracellular signal transduction / positive regulation of cell migration / membrane raft / protein heterodimerization activity / external side of plasma membrane / focal adhesion / Neutrophil degranulation / positive regulation of cell population proliferation / protein-containing complex binding / endoplasmic reticulum membrane / negative regulation of transcription by RNA polymerase II / signal transduction / extracellular space / extracellular exosome / extracellular region / nucleoplasm / membrane / identical protein binding / nucleus / plasma membrane / cytosol / cytoplasm
Similarity search - Function
Short hematopoietin receptor, family 2, conserved site / Short hematopoietin receptor family 2 signature. / Type I cytokine receptor, cytokine-binding domain / Interleukin-6 receptor alpha chain, binding / PDZ domain / Pdz3 Domain / PDZ domain / PDZ domain profile. / Domain present in PSD-95, Dlg, and ZO-1/2. / PDZ domain ...Short hematopoietin receptor, family 2, conserved site / Short hematopoietin receptor family 2 signature. / Type I cytokine receptor, cytokine-binding domain / Interleukin-6 receptor alpha chain, binding / PDZ domain / Pdz3 Domain / PDZ domain / PDZ domain profile. / Domain present in PSD-95, Dlg, and ZO-1/2. / PDZ domain / PDZ superfamily / Fibronectin type-III domain profile. / Fibronectin type III / Fibronectin type III superfamily / Roll / Immunoglobulin-like fold / Mainly Beta
Similarity search - Domain/homology
ACETATE ION / Syntenin-1 / Interleukin-5 receptor subunit alpha
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.7 Å
AuthorsKang, B.S. / Cooper, D.R. / Devedjiev, Y. / Derewenda, U. / Derewenda, Z.S.
CitationJournal: Structure / Year: 2003
Title: Molecular Roots of Degenerate Specificity in Syntenin'S Pdz2 Domain: Reassessment of the Pdz Recognition Paradigm
Authors: Kang, B.S. / Cooper, D.R. / Devedjiev, Y. / Derewenda, U. / Derewenda, Z.S.
History
DepositionJan 31, 2003Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jul 11, 2003Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3May 8, 2019Group: Advisory / Data collection ...Advisory / Data collection / Derived calculations / Experimental preparation / Other
Category: exptl_crystal_grow / pdbx_database_proc ...exptl_crystal_grow / pdbx_database_proc / pdbx_database_status / pdbx_struct_special_symmetry / pdbx_unobs_or_zero_occ_atoms
Item: _exptl_crystal_grow.method / _pdbx_database_status.recvd_author_approval
Revision 1.4Dec 13, 2023Group: Advisory / Data collection ...Advisory / Data collection / Database references / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / pdbx_unobs_or_zero_occ_atoms
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf
Remark 700 SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: SYNTENIN 1
B: SYNTENIN 1
P: INTERLEUKIN 5 RECEPTOR ALPHA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)37,2137
Polymers36,9763
Non-polymers2364
Water11,854658
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
Unit cell
Length a, b, c (Å)101.485, 48.172, 74.996
Angle α, β, γ (deg.)90.00, 120.24, 90.00
Int Tables number5
Space group name H-MC121
Components on special symmetry positions
IDModelComponents
11B-2246-

HOH

21P-2002-

HOH

DetailsTHE TRIMER IS FORMED BY THE COMPLEX OF CHAINS A AND BWITH ONE MOLECULE OF CHAIN P

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Components

#1: Protein SYNTENIN 1 / SYNDECAN BINDING PROTEIN 1 / MELANOMA DIFFERENTIATION ASSOCIATED PROTEIN-9 / MDA-9 / SCAFFOLD ...SYNDECAN BINDING PROTEIN 1 / MELANOMA DIFFERENTIATION ASSOCIATED PROTEIN-9 / MDA-9 / SCAFFOLD PROTEIN PBP1 / TACIP18 / PRO-TGF-ALPHA CYTOPLASMIC DOMAIN-INTERACTING PROTEIN 18


Mass: 18018.688 Da / Num. of mol.: 2 / Fragment: PDZ2, RESIDUES 113-273
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21 / References: UniProt: O00560
#2: Protein/peptide INTERLEUKIN 5 RECEPTOR ALPHA / IL-5R-ALPHA / CD125 ANTIGEN


Mass: 938.975 Da / Num. of mol.: 1 / Fragment: LAST 8 RESIDUES, RESIDUES 413-420 / Source method: obtained synthetically / Source: (synth.) HOMO SAPIENS (human) / References: UniProt: Q01344
#3: Chemical
ChemComp-ACT / ACETATE ION / Acetate


Mass: 59.044 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C2H3O2
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 658 / Source method: isolated from a natural source / Formula: H2O
Compound detailsMOL_ID 1: FUNCTIONS AS AN ADAPTER PROTEIN. MAY ALSO FUNCTION TO COUPLE SYNDECANS TO CYTOSKELETAL ...MOL_ID 1: FUNCTIONS AS AN ADAPTER PROTEIN. MAY ALSO FUNCTION TO COUPLE SYNDECANS TO CYTOSKELETAL TRANSCRIPTION PROTEINS OR SIGNALING COMPONENTS. ALSO SEEMS TO COUPLE FACTOR SOX4 TO THE IL-5 RECEPTOR (IL5RA) (MOL_ID 2 IN THIS ENTRY)

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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: 2.2 Å3/Da / Density % sol: 43.7 %
Crystal growMethod: vapor diffusion, sitting drop / pH: 4.6
Details: SITTING DROP WITH 0.2 M SODIUM ACETATE, PH 4.6 28% PEG4000, 0.2 M AMMONIUM ACETATE

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: NSLS / Beamline: X9B / Wavelength: 0.97946
DetectorType: ADSC CCD / Detector: CCD / Date: Jan 20, 2002
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97946 Å / Relative weight: 1
ReflectionResolution: 1.7→50 Å / Num. obs: 112090 / % possible obs: 95.7 % / Redundancy: 3.4 % / Rmerge(I) obs: 0.044 / Net I/σ(I): 25.4
Reflection shellResolution: 1.7→1.76 Å / Rmerge(I) obs: 0.287 / Mean I/σ(I) obs: 3.13 / % possible all: 72.4
Reflection
*PLUS
Highest resolution: 1.7 Å / Lowest resolution: 50 Å / Redundancy: 3.4 % / Rmerge(I) obs: 0.044
Reflection shell
*PLUS
Rmerge(I) obs: 0.287 / Mean I/σ(I) obs: 3.13

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Processing

Software
NameVersionClassification
REFMAC5.1.24refinement
HKL-2000data reduction
HKL-2000data scaling
AMoREphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1N99

1n99


Resolution: 1.7→64.55 Å / Cor.coef. Fo:Fc: 0.965 / Cor.coef. Fo:Fc free: 0.93 / SU B: 2.207 / SU ML: 0.073 / Cross valid method: THROUGHOUT / ESU R: 0.172 / ESU R Free: 0.117 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.213 1048 3.2 %RANDOM
Rwork0.148 ---
obs-32205 95.8 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL PLUS MASK
Displacement parametersBiso mean: 12.64 Å2
Baniso -1Baniso -2Baniso -3
1--0 Å20 Å2-0.01 Å2
2--0.02 Å20 Å2
3----0.03 Å2
Refinement stepCycle: LAST / Resolution: 1.7→64.55 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2522 0 16 658 3196
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0160.0212547
X-RAY DIFFRACTIONr_bond_other_d0.0020.022373
X-RAY DIFFRACTIONr_angle_refined_deg1.5071.9523428
X-RAY DIFFRACTIONr_angle_other_deg0.80735527
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.0595329
X-RAY DIFFRACTIONr_dihedral_angle_2_deg
X-RAY DIFFRACTIONr_dihedral_angle_3_deg
X-RAY DIFFRACTIONr_dihedral_angle_4_deg
X-RAY DIFFRACTIONr_chiral_restr0.0890.2406
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.022828
X-RAY DIFFRACTIONr_gen_planes_other0.0030.02468
X-RAY DIFFRACTIONr_nbd_refined0.2260.2461
X-RAY DIFFRACTIONr_nbd_other0.2540.22864
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other0.0820.21554
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.2030.2437
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.1510.223
X-RAY DIFFRACTIONr_symmetry_vdw_other0.3080.267
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.170.277
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it1.1531.51647
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it1.93222647
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it2.723900
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it4.3024.5781
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 1.7→1.74 Å / Total num. of bins used: 20 /
RfactorNum. reflection
Rfree0.33 51
Rwork0.212 1739
Refinement
*PLUS
Highest resolution: 1.7 Å
Solvent computation
*PLUS
Displacement parameters
*PLUS

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